UniProtKB - P00722 (BGAL_ECOLI)
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
- BLAST>sp|P00722|BGAL_ECOLI Beta-galactosidase OS=Escherichia coli (strain K12) OX=83333 GN=lacZ PE=1 SV=2 MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWR FAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENP TGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRA GENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAV LEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPK LWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEH HPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHG MVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVD PSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYA HAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDR QFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALD GKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQ WRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTP LRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTA HAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLG LGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNI SRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLV WCQK
- Align
- Format
- Add to basketAdded to basket
- History
- Other tutorials and videos
- Help video
- Feedback
Beta-galactosidase
lacZ
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Protein has several cofactor binding sites:- Mg2+, Mn2+Note: Binds 2 magnesium ions per monomer. Can also use manganese.
- Na+Note: Binds 1 sodium ion per monomer.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=0.04 mM for p-nitrophenyl beta-D-galactoside6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- KM=0.12 mM for o-nitrophenyl beta-D-galactoside6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- KM=34 µM for p-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- KM=140 µM for o-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- KM=940 µM for allolactose (with magnesium as cofactor and 30 degrees Celsius)6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- KM=1350 µM for lactose (with magnesium as cofactor and 30 degrees Celsius)6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- Vmax=30.9 µmol/min/mg enzyme with lactose as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- Vmax=49.7 µmol/min/mg enzyme with allolactose as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- Vmax=59.7 µmol/min/mg enzyme with p-nitrophenyl beta-D-galactoside as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
- Vmax=360 µmol/min/mg enzyme with o-nitrophenyl beta-D-galactoside as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. - Ref.14"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541. - Ref.16"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358. - Ref.18"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000. - Ref.19"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 103 | Substrate | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 202 | Sodium | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 202 | Substrate | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 358 | Transition state stabilizer | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 392 | Transition state stabilizer | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 417 | Magnesium 11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 419 | Magnesium 11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 462 | Proton donor1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 462 | Magnesium 11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 462 | Substrate | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 538 | Nucleophile1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 598 | Magnesium 21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 602 | Sodium; via carbonyl oxygen | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 605 | Sodium | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 605 | Substrate | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 1000 | Substrate | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 1000 | Important for ensuring that an appropriate proportion of lactose is converted to allolactose | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- alkali metal ion binding Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- beta-galactosidase activity Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- carbohydrate binding Source: InterPro
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- magnesium ion binding Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- lactose catabolic process Source: CACAO <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Glycosidase, Hydrolase |
| Ligand | Magnesium, Manganese, Metal-binding, Sodium |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:BETAGALACTOSID-MONOMER MetaCyc:BETAGALACTOSID-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.2.1.23 2026 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P00722 |
Protein family/group databases
Carbohydrate-Active enZymes More...CAZyi | GH2 Glycoside Hydrolase Family 2 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:lacZ Ordered Locus Names:b0344, JW0335 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Escherichia coli (strain K12) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83333 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Escherichia coli strain K12 genome database More...EcoGenei | EG10527 lacZ |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti
- beta-galactosidase complex Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 202 | D → E or N: Causes a significant decrease in binding affinity in the absence of monovalent cations or in the presence of potassium ions, but only a moderate decrease in the presence of sodium ions. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 202 | D → F: Obliterates all binding and catalysis. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 358 | H → D, F, L or N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 392 | H → E, F or K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 462 | E → H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 538 | E → Q: 10000-fold decrease in the beta-galactosidase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 541 | H → E, F or N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 602 | F → A: Decreases the stability of the loop 794-804. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 795 | G → A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 798 | E → A or L: The catalytic efficiency is not increased, when the sodium concentration increases. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 798 | E → D or Q: Small increase of the catalytic efficiency, when the sodium concentration increases. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1000 | W → F, G, L or T: Decreases affinity for substrate. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4603 |
Drug and drug target database More...DrugBanki | DB01920 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose DB02228 2-deoxy-2-fluoro-Beta-D-galactose DB04382 2-Deoxy-Beta-D-Galactose DB04155 2-Fluoro-2-Deoxy-Beta-D-Galactopyranosyl-Beta-D-Glucopyranose DB02632 4-nitrophenyl-beta-D-galactoside DB04116 Allolactose DB01885 D-Galctopyranosyl-1-On DB01862 Isopropyl beta-D-thiogalactopyranoside DB04465 Lactose |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000057650 | 2 – 1024 | Beta-galactosidaseAdd BLAST | 1023 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P00722 |
PRoteomics IDEntifications database More...PRIDEi | P00722 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"lac repressor-operator interaction. VI. The natural inducer of the lac operon."
Jobe A., Bourgeois S.
J. Mol. Biol. 69:397-408(1972) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION BY ALLOLACTOSE.
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"Three-dimensional structure of beta-galactosidase from E. coli."
Jacobson R.H., Zhang X.-J., Dubose R.F., Matthews B.W.
Nature 369:761-766(1994) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, SUBUNIT. - Ref.23"High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation."
Juers D.H., Jacobson R.H., Wigley D., Zhang X.-J., Huber R.E., Tronrud D.E., Matthews B.W.
Protein Sci. 9:1685-1699(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND SODIUM IONS. - Ref.24"A structural view of the action of Escherichia coli (lacZ) beta-galactosidase."
Juers D.H., Heightman T.D., Vasella A., McCarter J.D., Mackenzie L., Withers S.G., Matthews B.W.
Biochemistry 40:14781-14794(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, MUTAGENESIS OF GLU-538 AND PHE-602, REACTION MECHANISM. - Ref.25"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 3 | EBI-369998,EBI-369998 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-10081N |
Protein interaction database and analysis system More...IntActi | P00722, 76 interactors |
STRING: functional protein association networks More...STRINGi | 316407.85674486 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P00722 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 5 – 7 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 11 – 14 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 16 – 18 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 23 – 26 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 37 – 39 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 40 – 45 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 52 – 54 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 57 – 66 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 67 – 69 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 73 – 76 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 83 – 88 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 91 – 94 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 100 – 105 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 121 – 130 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 132 – 136 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 137 – 145 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 147 – 155 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 158 – 164 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 166 – 168 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 170 – 173 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 175 – 177 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 180 – 191 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 194 – 198 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 202 – 205 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 213 – 218 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 220 – 232 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 236 – 249 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 255 – 263 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 266 – 275 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 279 – 281 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 289 – 298 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 304 – 307 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 310 – 318 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 319 – 321 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 323 – 331 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 336 – 339 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 342 – 345 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 352 – 356 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 362 – 364 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 370 – 382 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 387 – 389 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 397 – 406 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 409 – 413 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 421 – 423 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 424 – 429 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 431 – 433 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 434 – 448 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 454 – 458 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 461 – 463 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 467 – 479 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 489 – 491 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 492 – 494 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 498 – 500 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 507 – 509 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 514 – 516 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 521 – 525 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 534 – 540 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 543 – 545 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 550 – 559 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 563 – 569 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 576 – 579 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 585 – 588 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 590 – 593 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 600 – 603 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 617 – 624 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 627 – 633 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 636 – 641 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 652 – 659 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 662 – 670 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 678 – 682 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 691 – 703 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 708 – 710 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 714 – 726 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 740 – 743 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 745 – 752 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 755 – 760 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 761 – 763 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 765 – 771 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 777 – 784 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 791 – 794 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 799 – 801 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 804 – 806 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 807 – 814 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 815 – 818 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 820 – 830 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 832 – 845 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 848 – 860 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 861 – 863 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 865 – 873 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 875 – 877 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 881 – 890 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 894 – 904 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 915 – 922 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 923 – 926 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 939 – 947 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 950 – 963 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 965 – 970 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 974 – 976 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 981 – 991 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 999 – 1001 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1006 – 1008 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1013 – 1022 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P00722 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P00722 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P00722 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 538 – 541 | Substrate binding | 4 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105CNT Bacteria COG3250 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000252443 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P00722 |
KEGG Orthology (KO) More...KOi | K01190 |
Identification of Orthologs from Complete Genome Data More...OMAi | PSNWQLQ |
Database for complete collections of gene phylogenies More...PhylomeDBi | P00722 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.120.260, 1 hit 2.60.40.10, 2 hits 2.70.98.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_01687 Beta_gal, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR004199 B-gal_small/dom_5 IPR036156 Beta-gal/glucu_dom_sf IPR011013 Gal_mutarotase_sf_dom IPR008979 Galactose-bd-like_sf IPR014718 GH-type_carb-bd IPR006101 Glyco_hydro_2 IPR023232 Glyco_hydro_2_AS IPR023933 Glyco_hydro_2_beta_Galsidase IPR006103 Glyco_hydro_2_cat IPR023230 Glyco_hydro_2_CS IPR006102 Glyco_hydro_2_Ig-like IPR006104 Glyco_hydro_2_N IPR017853 Glycoside_hydrolase_SF IPR013783 Ig-like_fold IPR032312 LacZ_4 |
The PANTHER Classification System More...PANTHERi | PTHR10066:SF76 PTHR10066:SF76, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF02929 Bgal_small_N, 1 hit PF16353 DUF4981, 1 hit PF00703 Glyco_hydro_2, 1 hit PF02836 Glyco_hydro_2_C, 1 hit PF02837 Glyco_hydro_2_N, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00132 GLHYDRLASE2 |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01038 Bgal_small_N, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF49303 SSF49303, 2 hits SSF49785 SSF49785, 1 hit SSF51445 SSF51445, 1 hit SSF74650 SSF74650, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00719 GLYCOSYL_HYDROL_F2_1, 1 hit PS00608 GLYCOSYL_HYDROL_F2_2, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ
60 70 80 90 100
QLRSLNGEWR FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI
110 120 130 140 150
YTNVTYPITV NPPFVPTENP TGCYSLTFNV DESWLQEGQT RIIFDGVNSA
160 170 180 190 200
FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA GENRLAVMVL RWSDGSYLED
210 220 230 240 250
QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV LEAEVQMCGE
260 270 280 290 300
LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK
310 320 330 340 350
LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL
360 370 380 390 400
LIRGVNRHEH HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY
410 420 430 440 450
TLCDRYGLYV VDEANIETHG MVPMNRLTDD PRWLPAMSER VTRMVQRDRN
460 470 480 490 500
HPSVIIWSLG NESGHGANHD ALYRWIKSVD PSRPVQYEGG GADTTATDII
510 520 530 540 550
CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA HAMGNSLGGF
560 570 580 590 600
AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
610 620 630 640 650
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN
660 670 680 690 700
ELLHWMVALD GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR
710 720 730 740 750
VVQPNATAWS EAGHISAWQQ WRLAENLSVT LPAASHAIPH LTTSEMDFCI
760 770 780 790 800
ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP LRDQFTRAPL DNDIGVSEAT
810 820 830 840 850
RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA HAWQHQGKTL
860 870 880 890 900
FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG
910 920 930 940 950
LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH
960 970 980 990 1000
QWRGDFQFNI SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW
1010 1020
SPSVSAEFQL SAGRYHYQLV WCQK
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | J01636 Genomic DNA Translation: AAA24053.1 V00296 Genomic DNA Translation: CAA23573.1 U73857 Genomic DNA Translation: AAB18068.1 U00096 Genomic DNA Translation: AAC73447.1 AP009048 Genomic DNA Translation: BAE76126.1 V00295 Genomic DNA Translation: CAA23570.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A90981 GBEC |
NCBI Reference Sequences More...RefSeqi | NP_414878.1, NC_000913.3 WP_000177906.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC73447; AAC73447; b0344 BAE76126; BAE76126; BAE76126 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 945006 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW0335 eco:b0344 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P00722 | Beta-galactosidase | 1024 | |||
| Beta-galactosidase | 1024 | ||||
| Beta-galactosidase | 1024 | ||||
| Beta-galactosidase | 1024 | ||||
| Beta-galactosidase | 1024 | ||||
| +10 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P00722 | Beta-galactosidase | 1024 | |||
| Beta-galactosidase | 1024 | ||||
| Beta-galactosidase | 1024 | ||||
| Beta-galactosidase | 1024 | ||||
| Beta-galactosidase | 1024 | ||||
| +1780 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P00722 | Beta-galactosidase | 1024 | |||
| Beta-galactosidase | 1024 | ||||
| Beta-galactosidase | 1024 | ||||
| Beta-galactosidase | 1024 | ||||
| Beta-galactosidase | 1024 | ||||
| +3830 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Worthington enzyme manual |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | J01636 Genomic DNA Translation: AAA24053.1 V00296 Genomic DNA Translation: CAA23573.1 U73857 Genomic DNA Translation: AAB18068.1 U00096 Genomic DNA Translation: AAC73447.1 AP009048 Genomic DNA Translation: BAE76126.1 V00295 Genomic DNA Translation: CAA23570.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A90981 GBEC |
NCBI Reference Sequences More...RefSeqi | NP_414878.1, NC_000913.3 WP_000177906.1, NZ_LN832404.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1DP0 | X-ray | 1.70 | A/B/C/D | 10-1024 | [»] | |
| 1F4A | X-ray | 2.80 | A/B/C/D | 4-1024 | [»] | |
| 1F4H | X-ray | 2.80 | A/B/C/D | 4-1024 | [»] | |
| 1HN1 | X-ray | 3.00 | A/B/C/D | 10-1024 | [»] | |
| 1JYN | X-ray | 1.80 | A/B/C/D | 10-1024 | [»] | |
| 1JYV | X-ray | 1.75 | A/B/C/D | 10-1024 | [»] | |
| 1JYW | X-ray | 1.55 | A/B/C/D | 10-1024 | [»] | |
| 1JYX | X-ray | 1.75 | A/B/C/D | 10-1024 | [»] | |
| 1JZ2 | X-ray | 2.10 | A/B/C/D | 2-1024 | [»] | |
| 1JZ3 | X-ray | 1.75 | A/B/C/D | 10-1024 | [»] | |
| 1JZ4 | X-ray | 2.10 | A/B/C/D | 10-1024 | [»] | |
| 1JZ5 | X-ray | 1.80 | A/B/C/D | 10-1024 | [»] | |
| 1JZ6 | X-ray | 2.10 | A/B/C/D | 10-1024 | [»] | |
| 1JZ7 | X-ray | 1.50 | A/B/C/D | 10-1024 | [»] | |
| 1JZ8 | X-ray | 1.50 | A/B/C/D | 10-1024 | [»] | |
| 1PX3 | X-ray | 1.60 | A/B/C/D | 10-1024 | [»] | |
| 1PX4 | X-ray | 1.60 | A/B/C/D | 10-1024 | [»] | |
| 3CZJ | X-ray | 2.05 | A/B/C/D | 10-1024 | [»] | |
| 3DYM | X-ray | 2.05 | A/B/C/D | 10-1024 | [»] | |
| 3DYO | X-ray | 1.80 | A/B/C/D | 10-1024 | [»] | |
| 3DYP | X-ray | 1.75 | A/B/C/D | 10-1024 | [»] | |
| 3E1F | X-ray | 3.00 | 1/2/3/4 | 10-1024 | [»] | |
| 3I3B | X-ray | 2.20 | A/B/C/D | 10-1024 | [»] | |
| 3I3D | X-ray | 2.20 | A/B/C/D | 10-1024 | [»] | |
| 3I3E | X-ray | 2.10 | A/B/C/D | 10-1024 | [»] | |
| 3IAP | X-ray | 2.00 | A/B/C/D | 10-1024 | [»] | |
| 3IAQ | X-ray | 2.70 | A/B/C/D | 10-1024 | [»] | |
| 3J7H | electron microscopy | 3.20 | A/B/C/D | 1-1024 | [»] | |
| 3MUY | X-ray | 2.50 | 1/2/3/4 | 10-1024 | [»] | |
| 3MUZ | X-ray | 1.90 | 1/2/3/4 | 10-1024 | [»] | |
| 3MV0 | X-ray | 2.20 | 1/2/3/4 | 10-1024 | [»] | |
| 3MV1 | X-ray | 2.20 | 1/2/3/4 | 10-1024 | [»] | |
| 3SEP | X-ray | 2.05 | A/B/C/D | 10-1024 | [»] | |
| 3T08 | X-ray | 2.00 | A/B/C/D | 10-1024 | [»] | |
| 3T09 | X-ray | 1.75 | A/B/C/D | 10-1024 | [»] | |
| 3T0A | X-ray | 1.90 | A/B/C/D | 10-1024 | [»] | |
| 3T0B | X-ray | 2.40 | A/B/C/D | 10-1024 | [»] | |
| 3T0D | X-ray | 1.93 | A/B/C/D | 10-1024 | [»] | |
| 3T2O | X-ray | 1.85 | A/B/C/D | 10-1024 | [»] | |
| 3T2P | X-ray | 2.60 | A/B/C/D | 10-1024 | [»] | |
| 3T2Q | X-ray | 2.40 | A/B/C/D | 10-1024 | [»] | |
| 3VD3 | X-ray | 2.80 | A/B/C/D | 10-1024 | [»] | |
| 3VD4 | X-ray | 2.00 | A/B/C/D | 10-1024 | [»] | |
| 3VD5 | X-ray | 2.70 | A/B/C/D | 10-1024 | [»] | |
| 3VD7 | X-ray | 2.87 | A/B/C/D | 10-1024 | [»] | |
| 3VD9 | X-ray | 2.05 | A/B/C/D | 10-1024 | [»] | |
| 3VDA | X-ray | 2.50 | A/B/C/D | 10-1024 | [»] | |
| 3VDB | X-ray | 2.05 | A/B/C/D | 10-1024 | [»] | |
| 3VDC | X-ray | 2.55 | A/B/C/D | 10-1024 | [»] | |
| 4CKD | electron microscopy | 13.00 | A/B/C/D | 1-1024 | [»] | |
| 4DUV | X-ray | 2.10 | A/B/C/D | 10-1024 | [»] | |
| 4DUW | X-ray | 2.20 | A/B/C/D | 10-1024 | [»] | |
| 4DUX | X-ray | 2.30 | A/B/C/D | 10-1024 | [»] | |
| 4TTG | X-ray | 1.60 | A/B/C/D | 15-1024 | [»] | |
| 4V40 | X-ray | 2.50 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P | 2-1024 | [»] | |
| 4V41 | X-ray | 2.50 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P | 2-1024 | [»] | |
| 4V44 | X-ray | 2.70 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P | 2-1024 | [»] | |
| 4V45 | X-ray | 2.60 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P | 2-1024 | [»] | |
| 5A1A | electron microscopy | 2.20 | A/B/C/D | 3-1024 | [»] | |
| 6CVM | electron microscopy | 1.90 | A/B/C/D | 3-1023 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P00722 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P00722 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-10081N |
Protein interaction database and analysis system More...IntActi | P00722, 76 interactors |
STRING: functional protein association networks More...STRINGi | 316407.85674486 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P00722 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4603 |
Drug and drug target database More...DrugBanki | DB01920 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose DB02228 2-deoxy-2-fluoro-Beta-D-galactose DB04382 2-Deoxy-Beta-D-Galactose DB04155 2-Fluoro-2-Deoxy-Beta-D-Galactopyranosyl-Beta-D-Glucopyranose DB02632 4-nitrophenyl-beta-D-galactoside DB04116 Allolactose DB01885 D-Galctopyranosyl-1-On DB01862 Isopropyl beta-D-thiogalactopyranoside DB04465 Lactose |
Protein family/group databases
Carbohydrate-Active enZymes More...CAZyi | GH2 Glycoside Hydrolase Family 2 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P00722 |
PRoteomics IDEntifications database More...PRIDEi | P00722 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC73447; AAC73447; b0344 BAE76126; BAE76126; BAE76126 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 945006 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW0335 eco:b0344 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0522 |
Escherichia coli strain K12 genome database More...EcoGenei | EG10527 lacZ |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105CNT Bacteria COG3250 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000252443 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P00722 |
KEGG Orthology (KO) More...KOi | K01190 |
Identification of Orthologs from Complete Genome Data More...OMAi | PSNWQLQ |
Database for complete collections of gene phylogenies More...PhylomeDBi | P00722 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:BETAGALACTOSID-MONOMER MetaCyc:BETAGALACTOSID-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.2.1.23 2026 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P00722 |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P00722 |
Protein Ontology More...PROi | PR:P00722 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.120.260, 1 hit 2.60.40.10, 2 hits 2.70.98.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_01687 Beta_gal, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR004199 B-gal_small/dom_5 IPR036156 Beta-gal/glucu_dom_sf IPR011013 Gal_mutarotase_sf_dom IPR008979 Galactose-bd-like_sf IPR014718 GH-type_carb-bd IPR006101 Glyco_hydro_2 IPR023232 Glyco_hydro_2_AS IPR023933 Glyco_hydro_2_beta_Galsidase IPR006103 Glyco_hydro_2_cat IPR023230 Glyco_hydro_2_CS IPR006102 Glyco_hydro_2_Ig-like IPR006104 Glyco_hydro_2_N IPR017853 Glycoside_hydrolase_SF IPR013783 Ig-like_fold IPR032312 LacZ_4 |
The PANTHER Classification System More...PANTHERi | PTHR10066:SF76 PTHR10066:SF76, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF02929 Bgal_small_N, 1 hit PF16353 DUF4981, 1 hit PF00703 Glyco_hydro_2, 1 hit PF02836 Glyco_hydro_2_C, 1 hit PF02837 Glyco_hydro_2_N, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00132 GLHYDRLASE2 |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01038 Bgal_small_N, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF49303 SSF49303, 2 hits SSF49785 SSF49785, 1 hit SSF51445 SSF51445, 1 hit SSF74650 SSF74650, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00719 GLYCOSYL_HYDROL_F2_1, 1 hit PS00608 GLYCOSYL_HYDROL_F2_2, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | BGAL_ECOLI | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P00722Primary (citable) accession number: P00722 Secondary accession number(s): Q2MC80 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 188 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene - Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
