UniProtKB - P76491 (5DNU_ECOLI)
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>sp|P76491|5DNU_ECOLI 5'-deoxynucleotidase YfbR OS=Escherichia coli (strain K12) OX=83333 GN=yfbR PE=1 SV=1 MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGNVNAER IALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMVPEELRDIFAPLI DEHAYSDEEKSLVKQADALCAYLKCLEELAAGNNEFLLAKTRLEATLEARRSQEMDYFME IFVPSFHLSLDEISQDSPLCommunity curation ()Add a publicationFeedback
Protein
5'-deoxynucleotidase YfbR
Gene
yfbR
Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:
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
Essential component of the deoxycytidine triphosphate (dCTP) pathway for de novo synthesis of thymidylate. Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates (dAMP, dGMP, dTMP, dUMP, dIMP and dCMP) and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates.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.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The deoxycytidine pathway for thymidylate synthesis in Escherichia coli."
Weiss B.
J. Bacteriol. 189:7922-7926(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN THE SYNTHESIS OF THYMIDYLATE. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- a 2'-deoxyribonucleoside 5'-phosphateEC:3.1.3.89
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- See the description of this molecule in ChEBI.
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<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
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Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Source: Rhea- Search for this reaction in UniProtKB.
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a 2'-deoxyribonucleoside 5'-phosphate- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=a 2'-deoxyribonucleoside- Search proteins in UniProtKB for this molecule.
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+phosphate- Search proteins in UniProtKB for this molecule.
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<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
Co2+
- Search proteins in UniProtKB for this molecule.
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Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Inhibited by both ribo- and deoxyribonucleoside di- and triphosphates.1 Publication
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
<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=0.012 mM for 5'-dAMP2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- KM=0.047 mM for 5'-dGMP2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- KM=0.008 mM for 5'-dTMP2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- KM=0.020 mM for 5'-dUMP2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- KM=0.017 mM for 5'-dIMP2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- KM=0.036 mM for 5'-dCMP2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- KM=2.09 mM for pNPP2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Vmax=0.71 µmol/min/mg enzyme with 5'-dAMP as substrate2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Vmax=0.46 µmol/min/mg enzyme with 5'-dGMP as substrate2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Vmax=0.37 µmol/min/mg enzyme with 5'-dTMP as substrate2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Vmax=0.54 µmol/min/mg enzyme with 5'-dUMP as substrate2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Vmax=0.56 µmol/min/mg enzyme with 5'-dIMP as substrate2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Vmax=0.53 µmol/min/mg enzyme with 5'-dCMP as substrate2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Vmax=1.32 µmol/min/mg enzyme with pNPP as substrate2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
pH dependencei
Optimum pH is 8.0.2 Publications
Manual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 | 18 | Appears to be important in orienting the phosphate for catalysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 | 33 | Cobalt; via tele nitrogen | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 | 33 | Substrate | 1 | |
| Metal bindingi | 68 | Cobalt; via tele nitrogen | 1 | |
| Metal bindingi | 69 | Cobalt | 1 | |
| Binding sitei | 69 | Substrate | 1 | |
| Metal bindingi | 137 | Cobalt | 1 | |
| Binding sitei | 137 | Substrate | 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
- 5'-deoxynucleotidase 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- cobalt ion binding Source: EcoCycInferred from direct assayi
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- nucleotide binding Source: UniProtKB-KW
GO - Biological processi
- dUMP biosynthetic process Source: EcoCyc
<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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.4"The deoxycytidine pathway for thymidylate synthesis in Escherichia coli."
Weiss B.
J. Bacteriol. 189:7922-7926(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN THE SYNTHESIS OF THYMIDYLATE.
- pyrimidine deoxyribonucleotide salvage Source: EcoCycInferred from mutant phenotypei
- Ref.4"The deoxycytidine pathway for thymidylate synthesis in Escherichia coli."
Weiss B.
J. Bacteriol. 189:7922-7926(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN THE SYNTHESIS OF THYMIDYLATE.
<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 | Hydrolase |
| Ligand | Cobalt, Copper, Manganese, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:G7185-MONOMER MetaCyc:G7185-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.3.5, 2026 3.1.3.89, 2026 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P76491 |
<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%5Fand%5Ftaxonomy%5Fsection">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: 5'-deoxynucleotidase YfbRUniRule annotationManual assertion according to rulesi (EC:3.1.3.89
Manual assertion according to rulesi )Alternative name(s): 5'-deoxyribonucleotidaseUniRule annotation Manual assertion according to rulesi Nucleoside 5'-monophosphate phosphohydrolaseUniRule annotation Manual assertion according to rulesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:yfbRUniRule annotation Manual assertion according to rulesi Ordered Locus Names:b2291, JW2288 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 |
|
<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
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Manual assertion according to rulesi
- Cytoplasm UniRule annotation
Other locations
- cytoplasm Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- cytoplasm Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
Keywords - Cellular componenti
Cytoplasm<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%5Fand%5Fbiotech%5Fsection">'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 | 18 | R → A: Shows negligible enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 30 | V → A: Shows reduced activity and affinity compared to the wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 33 | H → A: Shows negligible enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 68 | H → A: Shows negligible enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 69 | D → A: Shows negligible enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 72 | E → A: Shows negligible enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 72 | E → V: Shows wild-type activity and substrate affinity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 77 | D → A: Shows negligible enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 122 | E → A: Shows reduced activity and affinity compared to the wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 137 | D → A: Shows negligible enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 |
<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000095049 | 1 – 199 | 5'-deoxynucleotidase YfbRAdd BLAST | 199 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P76491 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P76491 |
PRoteomics IDEntifications database More...PRIDEi | P76491 |
<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer.
UniRule annotationManual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.5"Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli."
Zimmerman M.D., Proudfoot M., Yakunin A., Minor W.
J. Mol. Biol. 378:215-226(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
GO - Molecular functioni
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.3"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4262969, 28 interactors |
Database of interacting proteins More...DIPi | DIP-28107N |
Protein interaction database and analysis system More...IntActi | P76491, 2 interactors |
STRING: functional protein association networks More...STRINGi | 511145.b2291 |
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 | 6 – 10 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 11 – 15 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 30 – 51 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 22 | |
| Helixi | 58 – 67 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 | 68 – 71 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 72 – 75 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 93 – 105 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 110 – 112 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 113 – 120 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Turni | 121 – 123 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 127 – 150 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 24 | |
| Helixi | 154 – 156 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 157 – 169 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 173 – 182 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 184 – 186 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P76491 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P76491 |
<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
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 30 – 142 | HDPROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 113 |
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 | 18 – 19 | Substrate binding | 2 | |
| Regioni | 77 – 80 | 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
Belongs to the 5DNU family.UniRule annotation
Manual assertion according to rulesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG1896, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_084784_0_0_6 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P76491 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P76491 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00077, HDc, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_01100, 5DNU, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR003607, HD/PDEase_dom IPR022971, YfbR IPR039356, YfbR/HDDC2 |
The PANTHER Classification System More...PANTHERi | PTHR11845, PTHR11845, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00471, HDc, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51831, HD, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.
P76491-1 [UniParc]FASTAAdd to basketAdded to basket
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MKQSHFFAHL SRLKLINRWP LMRNVRTENV SEHSLQVAMV AHALAAIKNR
60 70 80 90 100
KFGGNVNAER IALLAMYHDA SEVLTGDLPT PVKYFNSQIA QEYKAIEKIA
110 120 130 140 150
QQKLVDMVPE ELRDIFAPLI DEHAYSDEEK SLVKQADALC AYLKCLEELA
160 170 180 190
AGNNEFLLAK TRLEATLEAR RSQEMDYFME IFVPSFHLSL DEISQDSPL
Length:199
Mass (Da):22,708
Last modified:February 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i895E9A06130DA057
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 | U00096 Genomic DNA Translation: AAC75351.1 AP009048 Genomic DNA Translation: BAE76684.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A65001 |
NCBI Reference Sequences More...RefSeqi | NP_416794.1, NC_000913.3 WP_000813859.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC75351; AAC75351; b2291 BAE76684; BAE76684; BAE76684 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 57728027 946771 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW2288 eco:b2291 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.4444 |
<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 | Source | |
|---|---|---|---|---|---|---|
| P76491 | 5'-deoxynucleotidase YfbR | 199 | UniRef100_C4ZVI4 | |||
| 5'-deoxynucleotidase YfbR | 199 | |||||
| Deoxyribonucleoside 5'-monophosphatase | 199 | |||||
| 5'-deoxynucleotidase YfbR | 199 | |||||
| 5'-deoxynucleotidase YfbR | 199 | |||||
| +21 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P76491 | 5'-deoxynucleotidase YfbR | 199 | UniRef90_Q0T2J6 | |||
| 5'-deoxynucleotidase YfbR | 199 | |||||
| 5'-deoxynucleotidase KPK_1466 | 199 | |||||
| 5'-deoxynucleotidase KPN78578_26370 | 199 | |||||
| 5'-deoxynucleotidase YfbR | 199 | |||||
| +677 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P76491 | 5'-deoxynucleotidase VC_1978 | 194 | UniRef50_Q9KQM0 | |||
| 5'-deoxynucleotidase VS_2195 | 194 | |||||
| 5'-deoxynucleotidase YfbR | 199 | |||||
| 5'-deoxynucleotidase YfbR | 199 | |||||
| 5'-deoxynucleotidase YfbR | 199 | |||||
| +2013 | ||||||
<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: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC75351.1 AP009048 Genomic DNA Translation: BAE76684.1 |
| PIRi | A65001 |
| RefSeqi | NP_416794.1, NC_000913.3 WP_000813859.1, 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 |
| 2PAQ | X-ray | 2.10 | A/B | 1-199 | [»] | |
| 2PAR | X-ray | 2.10 | A/B | 1-199 | [»] | |
| 2PAU | X-ray | 2.10 | A/B | 1-199 | [»] | |
| SMRi | P76491 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 4262969, 28 interactors |
| DIPi | DIP-28107N |
| IntActi | P76491, 2 interactors |
| STRINGi | 511145.b2291 |
Proteomic databases
| jPOSTi | P76491 |
| PaxDbi | P76491 |
| PRIDEi | P76491 |
Genome annotation databases
| EnsemblBacteriai | AAC75351; AAC75351; b2291 BAE76684; BAE76684; BAE76684 |
| GeneIDi | 57728027 946771 |
| KEGGi | ecj:JW2288 eco:b2291 |
| PATRICi | fig|1411691.4.peg.4444 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB3855 |
Phylogenomic databases
| eggNOGi | COG1896, Bacteria |
| HOGENOMi | CLU_084784_0_0_6 |
| InParanoidi | P76491 |
| PhylomeDBi | P76491 |
Enzyme and pathway databases
| BioCyci | EcoCyc:G7185-MONOMER MetaCyc:G7185-MONOMER |
| BRENDAi | 3.1.3.5, 2026 3.1.3.89, 2026 |
| SABIO-RKi | P76491 |
Miscellaneous databases
| EvolutionaryTracei | P76491 |
Protein Ontology More...PROi | PR:P76491 |
Family and domain databases
| CDDi | cd00077, HDc, 1 hit |
| HAMAPi | MF_01100, 5DNU, 1 hit |
| InterProi | View protein in InterPro IPR003607, HD/PDEase_dom IPR022971, YfbR IPR039356, YfbR/HDDC2 |
| PANTHERi | PTHR11845, PTHR11845, 1 hit |
| SMARTi | View protein in SMART SM00471, HDc, 1 hit |
| PROSITEi | View protein in PROSITE PS51831, HD, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | 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 | 5DNU_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 | P76491Primary (citable) accession number: P76491 Secondary accession number(s): Q2MAM2 | |
| <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 27, 2002 |
| Last sequence update: | February 1, 1997 | |
| Last modified: | April 7, 2021 | |
| This is version 155 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
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Uncharacterized protein families (UPF)
List of uncharacterized protein family (UPF) entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
