UniProtKB - Q05514 (MAAL_CLOTT)
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- BLAST>sp|Q05514|MAAL_CLOTT Methylaspartate ammonia-lyase OS=Clostridium tetanomorphum OX=1553 PE=1 SV=1 MKIVDVLCTPGLTGFYFDDQRAIKKGAGHDGFTYTGSTVTEGFTQVRQKGESISVLLVLE DGQVAHGDCAAVQYSGAGGRDPLFLAKDFIPVIEKEIAPKLIGREITNFKPMAEEFDKMT VNGNRLHTAIRYGITQAILDAVAKTRKVTMAEVIRDEYNPGAEINAVPVFAQSGDDRYDN VDKMIIKEADVLPHALINNVEEKLGLKGEKLLEYVKWLRDRIIKLRVREDYAPIFHIDVY GTIGAAFDVDIKAMADYIQTLAEAAKPFHLRIEGPMDVEDRQKQMEAMRDLRAELDGRGV DAELVADEWCNTVEDVKFFTDNKAGHMVQIKTPDLGGVNNIADAIMYCKANGMGAYCGGT CNETNRSAEVTTNIGMACGARQVLAKPGMGVDEGMMIVKNEMNRVLALVGRRK
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Methylaspartate ammonia-lyase
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>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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT. - Ref.8"Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids."
Raj H., Szymanski W., de Villiers J., Rozeboom H.J., Veetil V.P., Reis C.R., de Villiers M., Dekker F.J., de Wildeman S., Quax W.J., Thunnissen A.M., Feringa B.L., Janssen D.B., Poelarends G.J.
Nat. Chem. 4:478-484(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-73 AND LEU-384, COFACTOR, SUBUNIT.
<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>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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT. - Ref.8"Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids."
Raj H., Szymanski W., de Villiers J., Rozeboom H.J., Veetil V.P., Reis C.R., de Villiers M., Dekker F.J., de Wildeman S., Quax W.J., Thunnissen A.M., Feringa B.L., Janssen D.B., Poelarends G.J.
Nat. Chem. 4:478-484(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-73 AND LEU-384, COFACTOR, SUBUNIT.
<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
<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.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.7"The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step."
Asuncion M., Blankenfeldt W., Barlow J.N., Gani D., Naismith J.H.
J. Biol. Chem. 277:8306-8311(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, ACTIVE SITE, COFACTOR, SUBUNIT. - Ref.8"Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids."
Raj H., Szymanski W., de Villiers J., Rozeboom H.J., Veetil V.P., Reis C.R., de Villiers M., Dekker F.J., de Wildeman S., Quax W.J., Thunnissen A.M., Feringa B.L., Janssen D.B., Poelarends G.J.
Nat. Chem. 4:478-484(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-73 AND LEU-384, COFACTOR, SUBUNIT.
<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.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR.
<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=0.65 mM for L-threo-beta-methylaspartate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
- KM=0.67 mM for L-threo-beta-methylaspartate (with 50 mM of KCl at pH 9 and at 30 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
- KM=0.7 mM for mesaconate (with 20 mM of MgCl2 at pH 9 and at 30 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
- KM=1 mM for L-threo-beta-methylaspartate (with 20 mM of MgCl2 at pH 9 and at 30 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
- KM=2.3 mM for L-aspartate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
- KM=2.8 mM for L-threo-beta-methylaspartate (with 0.3 mM of KCl at pH 9 and at 30 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
- Vmax=2089 µmol/min/mg enzyme with L-threo-beta-methylaspartate as substrate (with 50 mM of KCl at pH 9 and at 30 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
- Vmax=309 µmol/min/mg enzyme with L-threo-beta-methylaspartate as substrate (with 0.3 mM of KCl at pH 9 and at 30 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
- Vmax=266 µmol/min/mg enzyme with L-threo-beta-methylaspartate as substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
- Vmax=2.5 µmol/min/mg enzyme with L-erythro-beta-methylaspartate as substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
- Vmax=2.4 µmol/min/mg enzyme with L-aspartate as substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
<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>pH dependencei
<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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
<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>Temperature dependencei
<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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.5"The purification and properties of beta-methylaspartase."
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.
J. Biol. Chem. 234:320-328(1959) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-glutamate degradation via mesaconate pathway
This protein is involved in step 2 of the subpathway that synthesizes acetate and pyruvate from L-glutamate.Proteins known to be involved in the 4 steps of the subpathway in this organism are:
- Glutamate mutase sigma subunit (glmS), Glutamate mutase epsilon subunit (glmE)
- Methylaspartate ammonia-lyase
- no protein annotated in this organism
- no protein annotated in this organism
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetate and pyruvate from L-glutamate, the pathway L-glutamate degradation via mesaconate pathway and in Amino-acid degradation.
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 | 172 | L-threo-beta-methylaspartateBy similarity | 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 | 194 | 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 | 238 | Magnesium2 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
| 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 | 273 | Magnesium2 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
| 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 | 307 | Magnesium2 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
| 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 | 329 | L-threo-beta-methylaspartate | 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 | 331 | Proton acceptor2 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
| 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 | 361 | L-threo-beta-methylaspartate | 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
- cobalamin binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- methylaspartate ammonia-lyase activity Source: UniProtKB-EC
<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
- glutamate catabolic process via L-citramalate Source: UniProtKB-UniPathway
<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 | Lyase |
| Ligand | Cobalamin, Cobalt, Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:MONOMER-1103 |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 4.3.1.2 1527 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00561; UER00618 |
<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 | Recommended name: Methylaspartate ammonia-lyase (EC:4.3.1.2)Short name: MAL Alternative name(s): 3-methylaspartase ammonia-lyase Beta-methylaspartase |
| <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 | Clostridium tetanomorphum |
| <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 | 1553 [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 › Terrabacteria group › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
<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 | 73 | Q → A: It has very broad nucleophile scope and excellent regio- and diastereoselectivity in the amination reaction. This mutation strongly moves the specificity of MAL away from ammonia and towards methylamine. It is highly enantioselective. 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 | 194 | H → A: Strong (160-fold) decrease of the catalytic efficiency for deamination and slight (1.8-fold) decrease of affinity binding for L-threo-beta-methylaspartate. 7-fold decrease of the catalytic efficiency for amination and 20-fold decrease of affinity binding for mesaconate. It does not show any major conformational changes. 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 | 194 | H → R: It abolishes deaminase and aminase activities and does not show any major conformational changes. 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 | 329 | Q → A: Very strong decrease of the catalytic efficiency for deamination, whereas the affinity binding for L-threo-beta-methylaspartate is not affected. Strong (240-fold) decrease of the catalytic efficiency for amination and slight (2.4-fold) decrease of affinity binding for mesaconate. It does not show any major conformational changes. 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 | 329 | Q → R: It abolishes deaminase and aminase activities and does not show any major conformational changes. 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 | 331 | K → A: It abolishes deaminase and aminase activities and does not show any major conformational changes. 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 | 331 | K → G: It abolishes deaminase and aminase activities and does not show any major conformational changes. 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 | 331 | K → H: It abolishes deaminase and aminase activities and does not show any major conformational changes. 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 | 331 | K → Q: It abolishes deaminase and aminase activities and does not show any major conformational changes. 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 | 331 | K → R: It abolishes deaminase and aminase activities and does not show any major conformational changes. 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 | 384 | L → A: It has very broad electrophile scope and excellent regio- and enantioselectivity in the amination reaction. 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
Drug and drug target database More...DrugBanki | DB03661 Cysteinesulfonic Acid |
<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 ‘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_0000084547 | 1 – 413 | Methylaspartate ammonia-lyaseAdd BLAST | 413 |
Proteomic databases
PRoteomics IDEntifications database More...PRIDEi | Q05514 |
<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.1"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.6"Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis."
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B., Feringa B.L., Poelarends G.J.
ChemBioChem 10:2236-2245(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY, ACTIVE SITE, SUBUNIT. - Ref.7"The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step."
Asuncion M., Blankenfeldt W., Barlow J.N., Gani D., Naismith J.H.
J. Biol. Chem. 277:8306-8311(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, ACTIVE SITE, COFACTOR, SUBUNIT. - Ref.8"Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids."
Raj H., Szymanski W., de Villiers J., Rozeboom H.J., Veetil V.P., Reis C.R., de Villiers M., Dekker F.J., de Wildeman S., Quax W.J., Thunnissen A.M., Feringa B.L., Janssen D.B., Poelarends G.J.
Nat. Chem. 4:478-484(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-73 AND LEU-384, COFACTOR, SUBUNIT.
<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 | 2 – 11 | 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 | 14 – 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 | 5 | |
| <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 | 20 – 24 | 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 | 28 – 30 | 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 | 33 – 36 | 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 | 44 – 49 | 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 – 59 | 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 | 64 – 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 | 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 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 86 – 96 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 98 – 101 | 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 | 109 – 118 | 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 | 128 – 146 | 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 | 19 | |
| <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 | 150 – 158 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 179 – 186 | 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 | 190 – 194 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 200 – 204 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 209 – 225 | 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 | 17 | |
| <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 | 234 – 238 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 242 – 246 | 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 | 247 – 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 | 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 | 251 – 265 | 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 | 270 – 273 | 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 | 281 – 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 | 18 | |
| <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 | 302 – 306 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 313 – 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 | 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 | 325 – 330 | 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 | 333 – 335 | 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 | 339 – 350 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 354 – 357 | 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 | 365 – 378 | 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 | 381 – 384 | 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 | 387 – 391 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 392 – 410 | 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 | 19 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q05514 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q05514 |
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 | Q05514 |
<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 | 360 – 361 | L-threo-beta-methylaspartate bindingBy similarity | 2 |
<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
Family and domain databases
Conserved Domains Database More...CDDi | cd03314 MAL, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.20.20.120, 1 hit 3.30.390.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR036849 Enolase-like_C_sf IPR029017 Enolase-like_N IPR034390 Enolase-like_superfamily IPR006395 Me_Asp_am_lyase IPR022662 MeAsp_NH4-lyase_C IPR022665 MeAsp_NH4-lyase_N |
Pfam protein domain database More...Pfami | View protein in Pfam PF07476 MAAL_C, 1 hit PF05034 MAAL_N, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF017107 MAL, 1 hit |
Structure-Function Linkage Database More...SFLDi | SFLDG00151 methylaspartate_ammonia-lyase, 1 hit SFLDS00001 Enolase, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51604 SSF51604, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01502 B_methylAsp_ase, 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.
10 20 30 40 50
MKIVDVLCTP GLTGFYFDDQ RAIKKGAGHD GFTYTGSTVT EGFTQVRQKG
60 70 80 90 100
ESISVLLVLE DGQVAHGDCA AVQYSGAGGR DPLFLAKDFI PVIEKEIAPK
110 120 130 140 150
LIGREITNFK PMAEEFDKMT VNGNRLHTAI RYGITQAILD AVAKTRKVTM
160 170 180 190 200
AEVIRDEYNP GAEINAVPVF AQSGDDRYDN VDKMIIKEAD VLPHALINNV
210 220 230 240 250
EEKLGLKGEK LLEYVKWLRD RIIKLRVRED YAPIFHIDVY GTIGAAFDVD
260 270 280 290 300
IKAMADYIQT LAEAAKPFHL RIEGPMDVED RQKQMEAMRD LRAELDGRGV
310 320 330 340 350
DAELVADEWC NTVEDVKFFT DNKAGHMVQI KTPDLGGVNN IADAIMYCKA
360 370 380 390 400
NGMGAYCGGT CNETNRSAEV TTNIGMACGA RQVLAKPGMG VDEGMMIVKN
410
EMNRVLALVG RRK
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 | S48141 Genomic DNA Translation: AAB24070.1 X70499 Genomic DNA Translation: CAA49911.1 X70695 Genomic DNA Translation: CAA50027.1 |
Protein sequence database of the Protein Information Resource More...PIRi | B44285 |
<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 |
|---|
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q05514 | Methylaspartate ammonia-lyase | 413 | |||
| UPI00025C5008 | 438 | ||||
| UPI000481411C | 413 | ||||
| Methylaspartate ammonia-lyase | 413 | ||||
| Methylaspartate ammonia-lyase | 413 | ||||
| +2 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q05514 | Methylaspartate ammonia-lyase | 413 | |||
| UPI00025C5009 | 438 | ||||
| UPI000481411C | 413 | ||||
| UPI000BE44899 | 413 | ||||
| Methylaspartate ammonia-lyase | 413 | ||||
| +14 | |||||
<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
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 | S48141 Genomic DNA Translation: AAB24070.1 X70499 Genomic DNA Translation: CAA49911.1 X70695 Genomic DNA Translation: CAA50027.1 |
Protein sequence database of the Protein Information Resource More...PIRi | B44285 |
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 |
| 1KCZ | X-ray | 1.90 | A/B | 1-413 | [»] | |
| 1KD0 | X-ray | 1.90 | A/B | 1-413 | [»] | |
| 3ZVH | X-ray | 1.99 | A/B | 1-413 | [»] | |
| 3ZVI | X-ray | 1.90 | A/B | 1-413 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q05514 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q05514 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Chemistry databases
Drug and drug target database More...DrugBanki | DB03661 Cysteinesulfonic Acid |
Proteomic databases
PRoteomics IDEntifications database More...PRIDEi | Q05514 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00561; UER00618 |
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:MONOMER-1103 |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 4.3.1.2 1527 |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q05514 |
Family and domain databases
Conserved Domains Database More...CDDi | cd03314 MAL, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.20.20.120, 1 hit 3.30.390.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR036849 Enolase-like_C_sf IPR029017 Enolase-like_N IPR034390 Enolase-like_superfamily IPR006395 Me_Asp_am_lyase IPR022662 MeAsp_NH4-lyase_C IPR022665 MeAsp_NH4-lyase_N |
Pfam protein domain database More...Pfami | View protein in Pfam PF07476 MAAL_C, 1 hit PF05034 MAAL_N, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF017107 MAL, 1 hit |
Structure-Function Linkage Database More...SFLDi | SFLDG00151 methylaspartate_ammonia-lyase, 1 hit SFLDS00001 Enolase, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51604 SSF51604, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01502 B_methylAsp_ase, 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 | MAAL_CLOTT | |
| <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 | Q05514Primary (citable) accession number: Q05514 | |
| <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: | February 1, 1995 |
| Last sequence update: | February 1, 1995 | |
| Last modified: | May 23, 2018 | |
| This is version 92 of the entry and version 1 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, Direct protein sequencingDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
