HCHA_STAA3
ID HCHA_STAA3 Reviewed; 292 AA.
AC Q2FJ89;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein/nucleic acid deglycase HchA {ECO:0000255|HAMAP-Rule:MF_01046};
DE EC=3.1.2.- {ECO:0000255|HAMAP-Rule:MF_01046};
DE EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01046};
DE EC=3.5.1.124 {ECO:0000255|HAMAP-Rule:MF_01046};
DE AltName: Full=Maillard deglycase {ECO:0000255|HAMAP-Rule:MF_01046};
GN Name=hchA {ECO:0000255|HAMAP-Rule:MF_01046};
GN OrderedLocusNames=SAUSA300_0536;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
CC -!- FUNCTION: Protein and nucleotide deglycase that catalyzes the
CC deglycation of the Maillard adducts formed between amino groups of
CC proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus,
CC functions as a protein deglycase that repairs methylglyoxal- and
CC glyoxal-glycated proteins, and releases repaired proteins and lactate
CC or glycolate, respectively. Deglycates cysteine, arginine and lysine
CC residues in proteins, and thus reactivates these proteins by reversing
CC glycation by glyoxals. Acts on early glycation intermediates
CC (hemithioacetals and aminocarbinols), preventing the formation of
CC Schiff bases and advanced glycation endproducts (AGE). Also functions
CC as a nucleotide deglycase able to repair glycated guanine in the free
CC nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus
CC involved in a major nucleotide repair system named guanine glycation
CC repair (GG repair), dedicated to reversing methylglyoxal and glyoxal
CC damage via nucleotide sanitization and direct nucleic acid repair.
CC Plays an important role in protecting cells from carbonyl stress.
CC {ECO:0000255|HAMAP-Rule:MF_01046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] =
CC H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) +
CC L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) +
CC L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] =
CC glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] =
CC glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] =
CC glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) +
CC lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate;
CC Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate;
CC Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate;
CC Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate +
CC H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP +
CC H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate +
CC H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP +
CC H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a
CC guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-
CC COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O
CC = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300,
CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445,
CC ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a
CC guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-
CC COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O
CC = a 2'-deoxyguanosine in DNA + glycolate + H(+);
CC Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01046};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. HchA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01046}.
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DR EMBL; CP000255; ABD21878.1; -; Genomic_DNA.
DR RefSeq; WP_000076404.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FJ89; -.
DR SMR; Q2FJ89; -.
DR MEROPS; C56.006; -.
DR EnsemblBacteria; ABD21878; ABD21878; SAUSA300_0536.
DR KEGG; saa:SAUSA300_0536; -.
DR HOGENOM; CLU_066933_0_0_9; -.
DR OMA; GEKTGFW; -.
DR Proteomes; UP000001939; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR GO; GO:0036524; F:protein deglycase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016790; F:thiolester hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_01046; Deglycase_HchA; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR InterPro; IPR017283; HchA.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR PIRSF; PIRSF037798; Chaperone_HchA; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; Hydrolase; Stress response.
FT CHAIN 1..292
FT /note="Protein/nucleic acid deglycase HchA"
FT /id="PRO_1000064283"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 190
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01046"
SQ SEQUENCE 292 AA; 32177 MW; 7ADA2635287373CD CRC64;
MSQDVNELSK QPTPDKAEDN AFFPSPYSLS QYTAPKTDFD GVEHKGAYKD GKWKVLMIAA
EERYVLLENG KMFSTGNHPV EMLLPLHHLM EAGFDVDVAT LSGYPVKLEL WAMPTEDEAV
ISTYNKLKEK LKQPKKLADV IKNELGPDSD YLSVFIPGGH AAVVGISESE DVQQTLDWAL
DNDRFIVTLC HGPAALLSAG LNREKSPLEG YSVCVFPDSL DEGANIEIGY LPGRLKWLVA
DLLTKQGLKV VNDDMTGRTL KDRKLLTGDS PLASNELGKL AVNEMLNAIQ NK
