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HCHA_STAAR
ID   HCHA_STAAR              Reviewed;         292 AA.
AC   Q6GJB7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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}; OrderedLocusNames=SAR0556;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG39577.1; -; Genomic_DNA.
DR   RefSeq; WP_000076413.1; NC_002952.2.
DR   AlphaFoldDB; Q6GJB7; -.
DR   SMR; Q6GJB7; -.
DR   KEGG; sar:SAR0556; -.
DR   HOGENOM; CLU_066933_0_0_9; -.
DR   OMA; PMYHLDK; -.
DR   OrthoDB; 1152952at2; -.
DR   Proteomes; UP000000596; 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_0000209418"
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;  32192 MW;  A1BD47D5BBD8ABA6 CRC64;
     MSQDVNKLSK QPTPDKAEDN AFFPSPYSLS QYTAPKTDFD GVEHKGAYKD GKWKVLMIAA
     EERYVLLENG KMFSTGNHPV EMLLPLHHLM EAGFDVDVAT LSGYPAKLEL WAMPTEDEAV
     ISTYNKLKEK LKQPKKLADV IKNELGPDSD YLSVFIPGGH AAVVGISESE DVQQTLDWAL
     ENDRFIVTLC HGPAALLSAG LNREKSPLEG YSVCVFPDSL DEGANIEIGY LPGRLKWLVA
     DLLTKQSLKV VNDDMTGRTL KDRKLLTGDS PLASNELGKL AVNEMLNAIQ NK
 
 
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