UniProtKB - P31658 (HCHA_ECOLI)
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>sp|P31658|HCHA_ECOLI Protein/nucleic acid deglycase 1 OS=Escherichia coli (strain K12) OX=83333 GN=hchA PE=1 SV=3 MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERY LPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFF EQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRF VISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGM NIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAGCommunity curation ()Add a publicationFeedback
Protein/nucleic acid deglycase 1
hchA
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.5"Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione."
Misra K., Banerjee A.B., Ray S., Ray M.
Biochem. J. 305:999-1003(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.6"Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures."
Sastry M.S.R., Korotkov K., Brodsky Y., Baneyx F.
J. Biol. Chem. 277:46026-46034(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A CHAPERONE, SUBUNIT, ACTIVITY REGULATION. - Ref.7"Characterization of the Escherichia coli YedU protein as a molecular chaperone."
Malki A., Kern R., Abdallah J., Richarme G.
Biochem. Biophys. Res. Commun. 301:430-436(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A CHAPERONE, SUBUNIT. - Ref.8"Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions."
Mujacic M., Bader M.W., Baneyx F.
Mol. Microbiol. 51:849-859(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A CHAPERONE, DISRUPTION PHENOTYPE. - Ref.10"Peptidase activity of the Escherichia coli Hsp31 chaperone."
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S., Mori H., Richarme G.
J. Biol. Chem. 280:14420-14426(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185. - Ref.11"Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31."
Mujacic M., Baneyx F.
Mol. Microbiol. 60:1576-1589(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN STRESS RESISTANCE. - Ref.12"Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli."
Mujacic M., Baneyx F.
Appl. Environ. Microbiol. 73:1014-1018(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN ACID STRESS RESISTANCE. - Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Miscellaneous
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.10"Peptidase activity of the Escherichia coli Hsp31 chaperone."
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S., Mori H., Richarme G.
J. Biol. Chem. 280:14420-14426(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185. - Ref.18"Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain."
Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H., Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.
J. Biol. Chem. 278:44552-44559(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS), PROTEOLYTIC ACTIVITY, MUTAGENESIS OF CYS-185.
Caution
<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
- H2OEC:4.2.1.130
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Manual assertion based on experiment ini
- Ref.5"Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione."
Misra K., Banerjee A.B., Ray S., Ray M.
Biochem. J. 305:999-1003(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
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Manual assertion based on experiment ini
- Ref.5"Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione."
Misra K., Banerjee A.B., Ray S., Ray M.
Biochem. J. 305:999-1003(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
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H2O- Search proteins in UniProtKB for this molecule.
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+methylglyoxal- Search proteins in UniProtKB for this molecule.
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=(R)-lactate- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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- H2OEC:3.5.1.124
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Manual assertion inferred by curator fromi
- Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
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Manual assertion inferred by curator fromi
- Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
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H2O- Search proteins in UniProtKB for this molecule.
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+Nω-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein]- Search proteins in UniProtKB for this molecule.
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Nω-(1-hydroxy-2-oxopropyl)-L-arginine residuezoom- Search proteins in UniProtKB for this molecule.
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=H+- Search proteins in UniProtKB for this molecule.
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L-arginine residuezoom- Search proteins in UniProtKB for this molecule.
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+lactate- Search proteins in UniProtKB for this molecule.
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- H2OEC:3.5.1.124
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Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
- Search proteins in UniProtKB for this EC number.
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Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
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H2O- Search proteins in UniProtKB for this molecule.
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+N6-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein]- Search proteins in UniProtKB for this molecule.
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N6-(1-hydroxy-2-oxopropyl)-L-lysine residuezoom- Search proteins in UniProtKB for this molecule.
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=H+- Search proteins in UniProtKB for this molecule.
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+L-lysyl-[protein]- Search proteins in UniProtKB for this molecule.
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L-lysine residuezoom- Search proteins in UniProtKB for this molecule.
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+lactate- Search proteins in UniProtKB for this molecule.
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- H2OEC:3.5.1.124
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Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
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Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
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H2O- Search proteins in UniProtKB for this molecule.
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+S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein]- Search proteins in UniProtKB for this molecule.
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S-(1-hydroxy-2-oxopropyl)-L-cysteine residuezoom- Search proteins in UniProtKB for this molecule.
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=H+- Search proteins in UniProtKB for this molecule.
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+L-cysteinyl-[protein]- Search proteins in UniProtKB for this molecule.
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L-cysteine residuezoom- Search proteins in UniProtKB for this molecule.
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+lactate- Search proteins in UniProtKB for this molecule.
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- H2OEC:3.5.1.124
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Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
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Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
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H2O- Search proteins in UniProtKB for this molecule.
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+Nω-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein]- Search proteins in UniProtKB for this molecule.
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Nω-(1-hydroxy-2-oxoethyl)-L-arginine residuezoom- Search proteins in UniProtKB for this molecule.
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=glycolate- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+L-arginyl-[protein]- Search proteins in UniProtKB for this molecule.
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L-arginine residuezoom- Search proteins in UniProtKB for this molecule.
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- H2OEC:3.5.1.124
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Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
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H2O- Search proteins in UniProtKB for this molecule.
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+N6-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein]- Search proteins in UniProtKB for this molecule.
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N6-(1-hydroxy-2-oxoethyl)-L-lysine residuezoom- Search proteins in UniProtKB for this molecule.
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=glycolate- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+L-lysyl-[protein]- Search proteins in UniProtKB for this molecule.
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L-lysine residuezoom- Search proteins in UniProtKB for this molecule.
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- H2OEC:3.5.1.124
- Search proteins in UniProtKB for this molecule.
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Manual assertion inferred by curator fromi
- Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion inferred by curator fromi
- Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Manual assertion based on experiment ini
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
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H2O- Search proteins in UniProtKB for this molecule.
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+S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein]- Search proteins in UniProtKB for this molecule.
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S-(1-hydroxy-2-oxoethyl)-L-cysteine residuezoom- Search proteins in UniProtKB for this molecule.
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=glycolate- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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L-cysteine residuezoom- Search proteins in UniProtKB for this molecule.
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- H2O
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Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
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H2O- Search proteins in UniProtKB for this molecule.
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+N2-(1-hydroxy-2-oxopropyl)-dGTP- Search proteins in UniProtKB for this molecule.
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=dGTP- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+lactate- Search proteins in UniProtKB for this molecule.
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- H2O
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Manual assertion based on experiment ini
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
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+N2-(1-hydroxy-2-oxopropyl)-GTP- Search proteins in UniProtKB for this molecule.
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=GTP- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+lactate- Search proteins in UniProtKB for this molecule.
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- H2O
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Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
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+N2-(1-hydroxy-2-oxopropyl)-GDP- Search proteins in UniProtKB for this molecule.
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=GDP- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+lactate- Search proteins in UniProtKB for this molecule.
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- H2O
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- See the description of this molecule in ChEBI.
Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
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+N2-(1-hydroxy-2-oxopropyl)-GMP- Search proteins in UniProtKB for this molecule.
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=GMP- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+lactate- Search proteins in UniProtKB for this molecule.
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- H2O
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- See the description of this molecule in ChEBI.
Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
+N2-(1-hydroxy-2-oxoethyl)-dGTP- Search proteins in UniProtKB for this molecule.
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=dGTP- Search proteins in UniProtKB for this molecule.
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+glycolate- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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- H2O
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Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
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+N2-(1-hydroxy-2-oxoethyl)-GTP- Search proteins in UniProtKB for this molecule.
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=glycolate- Search proteins in UniProtKB for this molecule.
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+GTP- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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- H2O
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- See the description of this molecule in ChEBI.
Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
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+N2-(1-hydroxy-2-oxoethyl)-GDP- Search proteins in UniProtKB for this molecule.
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=GDP- Search proteins in UniProtKB for this molecule.
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+glycolate- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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- H2O
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- See the description of this molecule in ChEBI.
Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
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+N2-(1-hydroxy-2-oxoethyl)-GMP- Search proteins in UniProtKB for this molecule.
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=glycolate- Search proteins in UniProtKB for this molecule.
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+GMP- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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- an N2-(1-hydroxy-2-oxopropyl)-guanosine in RNA
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
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an N2-(1-hydroxy-2-oxopropyl)-guanosine in RNA- Search proteins in UniProtKB for this molecule.
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N2-(1-hydroxy-2-oxopropyl)-GMP residuezoom- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=a guanosine in RNA- Search proteins in UniProtKB for this molecule.
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GMP residuezoom- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+lactate- Search proteins in UniProtKB for this molecule.
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- an N2-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA
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Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
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an N2-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA- Search proteins in UniProtKB for this molecule.
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N2-(1-hydroxy-2-oxopropyl)-dGMP residuezoom- 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'-deoxyguanosine in DNA- Search proteins in UniProtKB for this molecule.
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dGMP residuezoom- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+H+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+lactate- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
zoom
- an N2-(1-hydroxy-2-oxoethyl)-guanosine in RNA
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
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Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
an N2-(1-hydroxy-2-oxoethyl)-guanosine in RNA- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
N2-(1-hydroxy-2-oxoethyl)-GMP residuezoom- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=a guanosine in RNA- Search proteins in UniProtKB for this molecule.
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GMP residuezoom- Search proteins in UniProtKB for this molecule.
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+glycolate- Search proteins in UniProtKB for this molecule.
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zoom
+H+- Search proteins in UniProtKB for this molecule.
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- an N2-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA
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- See the description of this molecule in ChEBI.
Manual assertion inferred by curator fromi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
an N2-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA- Search proteins in UniProtKB for this molecule.
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N2-(1-hydroxy-2-oxoethyl)-dGMP residuezoom- 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'-deoxyguanosine in DNA- Search proteins in UniProtKB for this molecule.
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dGMP residuezoom- Search proteins in UniProtKB for this molecule.
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+glycolate- Search proteins in UniProtKB for this molecule.
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zoom
+H+- Search proteins in UniProtKB for this molecule.
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<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
Manual assertion based on experiment ini
- Ref.5"Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione."
Misra K., Banerjee A.B., Ray S., Ray M.
Biochem. J. 305:999-1003(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.6"Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures."
Sastry M.S.R., Korotkov K., Brodsky Y., Baneyx F.
J. Biol. Chem. 277:46026-46034(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A CHAPERONE, SUBUNIT, ACTIVITY REGULATION. - Ref.10"Peptidase activity of the Escherichia coli Hsp31 chaperone."
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S., Mori H., Richarme G.
J. Biol. Chem. 280:14420-14426(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185. - Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, 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
Manual assertion based on experiment ini
- Ref.10"Peptidase activity of the Escherichia coli Hsp31 chaperone."
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S., Mori H., Richarme G.
J. Biol. Chem. 280:14420-14426(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185. - Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=55 µM for Lys-AMC (at 37 degrees Celsius and pH 8.5)1 Publication
Manual assertion based on experiment ini
- Ref.10"Peptidase activity of the Escherichia coli Hsp31 chaperone."
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S., Mori H., Richarme G.
J. Biol. Chem. 280:14420-14426(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185.
- KM=95 µM for Arg-AMC (at 37 degrees Celsius and pH 8.5)1 Publication
Manual assertion based on experiment ini
- Ref.10"Peptidase activity of the Escherichia coli Hsp31 chaperone."
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S., Mori H., Richarme G.
J. Biol. Chem. 280:14420-14426(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185.
- KM=120 µM for Ala-AMC (at 37 degrees Celsius and pH 8.5)1 Publication
Manual assertion based on experiment ini
- Ref.10"Peptidase activity of the Escherichia coli Hsp31 chaperone."
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S., Mori H., Richarme G.
J. Biol. Chem. 280:14420-14426(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185.
- KM=1.43 mM for methylglyoxal1 Publication
Manual assertion based on experiment ini
- Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
pH dependencei
Manual assertion based on experiment ini
- Ref.5"Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione."
Misra K., Banerjee A.B., Ray S., Ray M.
Biochem. J. 305:999-1003(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.10"Peptidase activity of the Escherichia coli Hsp31 chaperone."
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S., Mori H., Richarme G.
J. Biol. Chem. 280:14420-14426(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185. - Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Temperature dependencei
Manual assertion based on experiment ini
- Ref.10"Peptidase activity of the Escherichia coli Hsp31 chaperone."
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S., Mori H., Richarme G.
J. Biol. Chem. 280:14420-14426(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185. - Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 | 86 | Zinc1 Publication Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 91 | Zinc1 Publication Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 123 | Zinc1 Publication Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 | 185 | NucleophileCurated | 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
- glyoxalase III 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.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Source: UniProtKB-UniRule
- protein deglycase activity Source: EcoCycInferred from direct assayi
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
- thiolester hydrolase activity Source: UniProtKB-UniRule
- zinc ion binding Source: UniProtKB-UniRule
GO - Biological processi
- DNA repair 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.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
- guanine deglycation Source: EcoCycInferred from direct assayi
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
- methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione Source: EcoCycInferred from mutant phenotypei
- Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- protein deglycation Source: EcoCycInferred from mutant phenotypei
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
- protein repair Source: EcoCycInferred from direct assayi
- Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
- response to acidic pH Source: EcoCycInferred from mutant phenotypei
- Ref.12"Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli."
Mujacic M., Baneyx F.
Appl. Environ. Microbiol. 73:1014-1018(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN ACID STRESS RESISTANCE.
- response to methylglyoxal Source: EcoCycInferred from mutant phenotypei
- Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- RNA repair Source: EcoCycInferred from mutant phenotypei
- Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
<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 | Chaperone, Hydrolase, Lyase |
Biological process | DNA damage, DNA repair, Stress response |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:G7055-MONOMER MetaCyc:G7055-MONOMER |
Protein family/group databases
MoonProt database of moonlighting proteins More...MoonProti | P31658 |
<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: Protein/nucleic acid deglycase 12 PublicationsManual assertion inferred by curator fromi
Manual assertion based on experiment ini
Manual assertion based on experiment ini
Manual assertion based on experiment ini
Alternative name(s): Glyoxalase III2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Holding molecular chaperone1 Publication Manual assertion based on opinion ini
Hsp311 Publication Manual assertion based on opinion ini
Maillard deglycase1 Publication Manual assertion based on opinion ini
|
<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:hchA Synonyms:yedU, yzzC Ordered Locus Names:b1967, JW1950 |
<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
GO - Cellular componenti
- cytosol Source: EcoCycInferred from direct assayi
- "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth."
Lopez-Campistrous A., Semchuk P., Burke L., Palmer-Stone T., Brokx S.J., Broderick G., Bottorff D., Bolch S., Weiner J.H., Ellison M.J.
Mol. Cell. Proteomics 4:1205-1209(2005) [PubMed] [Europe PMC] [Abstract] - "Protein abundance profiling of the Escherichia coli cytosol."
Ishihama Y., Schmidt T., Rappsilber J., Mann M., Hartl F.U., Kerner M.J., Frishman D.
BMC Genomics 9:102-102(2008) [PubMed] [Europe PMC] [Abstract]
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
<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
Manual assertion based on experiment ini
- Ref.8"Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions."
Mujacic M., Bader M.W., Baneyx F.
Mol. Microbiol. 51:849-859(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A CHAPERONE, DISRUPTION PHENOTYPE. - Ref.10"Peptidase activity of the Escherichia coli Hsp31 chaperone."
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S., Mori H., Richarme G.
J. Biol. Chem. 280:14420-14426(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185. - Ref.13"Hsp31 of Escherichia coli K-12 is glyoxalase III."
Subedi K.P., Choi D., Kim I., Min B., Park C.
Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.15"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.16"The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
Abdallah J., Mihoub M., Gautier V., Richarme G.
Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. - Ref.17"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs."
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
Science 357:208-211(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
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 | 77 | E → A: Loss of glyoxalase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 185 | C → A: Loss of glyoxalase and aminopeptidase activities. 3 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 186 | H → A: Shows approximately 17% remaining glyoxalase activity compared with that of the wild-type. 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication Manual assertion based on experiment ini
| |||
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000209412 | 2 – 283 | Protein/nucleic acid deglycase 1Add BLAST | 282 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P31658 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P31658 |
PRoteomics IDEntifications database More...PRIDEi | P31658 |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P31658 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<p>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.
3 PublicationsManual assertion based on experiment ini
- Ref.5"Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione."
Misra K., Banerjee A.B., Ray S., Ray M.
Biochem. J. 305:999-1003(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.6"Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures."
Sastry M.S.R., Korotkov K., Brodsky Y., Baneyx F.
J. Biol. Chem. 277:46026-46034(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A CHAPERONE, SUBUNIT, ACTIVITY REGULATION. - Ref.7"Characterization of the Escherichia coli YedU protein as a molecular chaperone."
Malki A., Kern R., Abdallah J., Richarme G.
Biochem. Biophys. Res. Commun. 301:430-436(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A CHAPERONE, SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
P31658
With | #Exp. | IntAct |
---|---|---|
asnC [P0ACI6] | 2 | EBI-909144,EBI-1133670 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4260394, 23 interactors 850832, 1 interactor |
Database of interacting proteins More...DIPi | DIP-11851N |
Protein interaction database and analysis system More...IntActi | P31658, 32 interactors |
STRING: functional protein association networks More...STRINGi | 511145.b1967 |
<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 <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 | 8 – 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 | 4 | |
Beta strandi | 18 – 20 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<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 | 23 – 29 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 50 – 54 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 60 – 62 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 68 – 70 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 75 – 87 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
Beta strandi | 92 – 99 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 106 – 108 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 116 – 128 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
Helixi | 133 – 138 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 145 – 151 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 155 – 158 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 161 – 163 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 165 – 176 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Beta strandi | 180 – 184 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 187 – 194 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 195 – 197 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<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 | 200 – 203 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 211 – 215 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Turni | 216 – 221 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 222 – 225 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 227 – 229 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 231 – 237 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 251 – 254 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 257 – 262 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 263 – 265 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 266 – 281 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 16 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P31658 |
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 | P31658 |
<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
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
Manual assertion based on experiment ini
- Ref.9"The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures."
Sastry M.S.R., Quigley P.M., Hol W.G.J., Baneyx F.
Proc. Natl. Acad. Sci. U.S.A. 101:8587-8592(2004) [PubMed] [Europe PMC] [Abstract]Cited for: DOMAIN.
<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
<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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG0693, Bacteria |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P31658 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.50.880, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_01046, Deglycase_HchA, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029062, Class_I_gatase-like IPR017283, HchA |
The PANTHER Classification System More...PANTHERi | PTHR43824:SF8, PTHR43824:SF8, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF037798, Chaperone_HchA, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52317, SSF52317, 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.
<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MTVQTSKNPQ VDIAEDNAFF PSEYSLSQYT SPVSDLDGVD YPKPYRGKHK
60 70 80 90 100
ILVIAADERY LPTDNGKLFS TGNHPIETLL PLYHLHAAGF EFEVATISGL
110 120 130 140 150
MTKFEYWAMP HKDEKVMPFF EQHKSLFRNP KKLADVVASL NADSEYAAIF
160 170 180 190 200
VPGGHGALIG LPESQDVAAA LQWAIKNDRF VISLCHGPAA FLALRHGDNP
210 220 230 240 250
LNGYSICAFP DAADKQTPEI GYMPGHLTWY FGEELKKMGM NIINDDITGR
260 270 280
VHKDRKLLTG DSPFAANALG KLAAQEMLAA YAG
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: AAC75033.1 AP009048 Genomic DNA Translation: BAA15794.1 |
Protein sequence database of the Protein Information Resource More...PIRi | C64961 |
NCBI Reference Sequences More...RefSeqi | NP_416476.1, NC_000913.3 WP_000218212.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC75033; AAC75033; b1967 BAA15794; BAA15794; BAA15794 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 946481 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW1950 eco:b1967 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.283 |
<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 | |
---|---|---|---|---|---|---|
P31658 | Protein/nucleic acid deglycase HchA | 283 | UniRef100_C4ZQN7 | |||
Protein/nucleic acid deglycase HchA | 283 | |||||
Protein/nucleic acid deglycase HchA | 283 | |||||
Protein/nucleic acid deglycase HchA | 283 | |||||
Protein/nucleic acid deglycase HchA | 283 | |||||
+52 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P31658 | Protein/nucleic acid deglycase HchA | 283 | UniRef90_Q8XB78 | |||
Protein/nucleic acid deglycase HchA | 283 | |||||
Protein/nucleic acid deglycase HchA | 283 | |||||
Protein/nucleic acid deglycase HchA | 283 | |||||
Protein/nucleic acid deglycase HchA | 283 | |||||
+840 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P31658 | Protein/nucleic acid deglycase HchA | 283 | UniRef50_Q8XB78 | |||
Protein/nucleic acid deglycase HchA | 283 | |||||
Protein/nucleic acid deglycase HchA | 283 | |||||
Protein/nucleic acid deglycase HchA | 283 | |||||
Protein/nucleic acid deglycase HchA | 283 | |||||
+1012 |
<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: AAC75033.1 AP009048 Genomic DNA Translation: BAA15794.1 |
PIRi | C64961 |
RefSeqi | NP_416476.1, NC_000913.3 WP_000218212.1, 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 |
1IZY | X-ray | 2.80 | A/B | 1-283 | [»] | |
1IZZ | X-ray | 2.31 | A | 1-283 | [»] | |
1N57 | X-ray | 1.60 | A | 1-283 | [»] | |
1ONS | X-ray | 2.20 | A | 2-283 | [»] | |
1PV2 | X-ray | 2.71 | A/B/C/D/E/F/G/H | 1-283 | [»] | |
SMRi | P31658 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260394, 23 interactors 850832, 1 interactor |
DIPi | DIP-11851N |
IntActi | P31658, 32 interactors |
STRINGi | 511145.b1967 |
Protein family/group databases
MoonProti | P31658 |
2D gel databases
SWISS-2DPAGEi | P31658 |
Proteomic databases
jPOSTi | P31658 |
PaxDbi | P31658 |
PRIDEi | P31658 |
Genome annotation databases
EnsemblBacteriai | AAC75033; AAC75033; b1967 BAA15794; BAA15794; BAA15794 |
GeneIDi | 946481 |
KEGGi | ecj:JW1950 eco:b1967 |
PATRICi | fig|1411691.4.peg.283 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB1705 |
Phylogenomic databases
eggNOGi | COG0693, Bacteria |
InParanoidi | P31658 |
Enzyme and pathway databases
BioCyci | EcoCyc:G7055-MONOMER MetaCyc:G7055-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P31658 |
Protein Ontology More...PROi | PR:P31658 |
Family and domain databases
Gene3Di | 3.40.50.880, 1 hit |
HAMAPi | MF_01046, Deglycase_HchA, 1 hit |
InterProi | View protein in InterPro IPR029062, Class_I_gatase-like IPR017283, HchA |
PANTHERi | PTHR43824:SF8, PTHR43824:SF8, 1 hit |
PIRSFi | PIRSF037798, Chaperone_HchA, 1 hit |
SUPFAMi | SSF52317, SSF52317, 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 | HCHA_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 | P31658Primary (citable) accession number: P31658 Secondary accession number(s): P76338 | |
<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: | July 1, 1993 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 170 of the entry and version 3 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, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Peptidase families
Classification of peptidase families and list of entries