HAMAP rule MF_01046
General rule information
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Accession | MF_01046 |
Dates | 13-FEB-2003 (Created)
19-NOV-2022 (Last updated, Version 31) |
Name | Deglycase_HchA |
Scope(s) |
Bacteria Staphylococcus Gammaproteobacteria |
Template(s) | P31658 (HCHA_ECOLI); [ Recover all ] |
Triggered by |
HAMAP; MF_01046 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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RecName: Full=Protein/nucleic acid deglycase HchA;<br /> EC=<a href="https://enzyme.expasy.org/EC/3.1.2.-">3.1.2.-</a>;<br /> EC=<a href="https://enzyme.expasy.org/EC/3.5.1.-">3.5.1.-</a>;<br /> EC=<a href="https://enzyme.expasy.org/EC/3.5.1.124">3.5.1.124</a>;<br /> AltName: Full=Maillard deglycase; | |
Gene name | Name=hchA; |
Comments
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FUNCTION | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. |
CATALYTIC ACTIVITY | Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; |
CATALYTIC ACTIVITY | Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA- COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; |
CATALYTIC ACTIVITY | Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA- COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; |
CATALYTIC ACTIVITY | Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; |
CATALYTIC ACTIVITY | Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; |
CATALYTIC ACTIVITY | Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; |
CATALYTIC ACTIVITY | Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; |
CATALYTIC ACTIVITY | Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; |
CATALYTIC ACTIVITY | Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; |
CATALYTIC ACTIVITY | Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; |
CATALYTIC ACTIVITY | Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; |
CATALYTIC ACTIVITY | Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; |
CATALYTIC ACTIVITY | Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; |
CATALYTIC ACTIVITY | Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; |
CATALYTIC ACTIVITY | Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA- COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; |
CATALYTIC ACTIVITY | Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; |
CATALYTIC ACTIVITY | Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA- COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; |
CATALYTIC ACTIVITY | Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; |
case <OC:Enterobacterales> | |
SUBUNIT | Homodimer. |
end case | |
SUBCELLULAR LOCATION | Cytoplasm. |
case <OC:Escherichia> or <OC:Shigella> | |
INDUCTION | By heat shock. |
end case | |
SIMILARITY | Belongs to the peptidase C56 family. HchA subfamily. |
Keywords
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Cytoplasm | |
DNA damage | |
DNA repair | |
Hydrolase | |
Stress response | |
case <FTGroup:1> | |
Metal-binding | |
Zinc | |
end case |
Gene Ontology
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GO:0016790; Molecular function:thiolester hydrolase activity | |
GO:0016811; Molecular function:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides | |
GO:0036524; Molecular function:protein deglycase activity | |
case <FTGroup:1> | |
GO:0008270; Molecular function:zinc ion binding | |
end case | |
GO:0006281; Biological process:DNA repair | |
GO:0030091; Biological process:protein repair | |
GO:0005737; Cellular component:cytoplasm |
Cross-references
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Pfam | PF01965; DJ-1_PfpI; 1; |
PIRSF | PIRSF037798; Chaperone_HchA; 1; |
Features
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From: HCHA_ECOLI (P31658) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 185 | 185 | /note="Nucleophile" | C | ||||||||
BINDING | 86 | 86 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
[H] | 1 | |||||||
BINDING | 91 | 91 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
[E] | 1 | |||||||
BINDING | 123 | 123 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
[H] | 1 |
Additional information
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Size range | 282-292 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |