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HCHA_SHIF8
ID   HCHA_SHIF8              Reviewed;         283 AA.
AC   Q0T3G3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=SFV_2012;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(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   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}.
CC   -!- INDUCTION: By heat shock. {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; CP000266; ABF04152.1; -; Genomic_DNA.
DR   RefSeq; WP_000218218.1; NC_008258.1.
DR   AlphaFoldDB; Q0T3G3; -.
DR   SMR; Q0T3G3; -.
DR   EnsemblBacteria; ABF04152; ABF04152; SFV_2012.
DR   GeneID; 58391644; -.
DR   KEGG; sfv:SFV_2012; -.
DR   HOGENOM; CLU_066933_0_0_6; -.
DR   OMA; PMYHLDK; -.
DR   BioCyc; SFLE373384:SFV_RS11275-MON; -.
DR   Proteomes; UP000000659; 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:0008270; F:zinc ion binding; 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; IPR017283; HchA.
DR   PIRSF; PIRSF037798; Chaperone_HchA; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Hydrolase; Metal-binding;
KW   Stress response; Zinc.
FT   CHAIN           1..283
FT                   /note="Protein/nucleic acid deglycase HchA"
FT                   /id="PRO_1000064280"
FT   ACT_SITE        185
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01046"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01046"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01046"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01046"
SQ   SEQUENCE   283 AA;  31280 MW;  55985ECD581821B2 CRC64;
     MTVQTSKNPQ VDIAEDNAFF PSEYSLSQYT SPVSDLDGVD YPKPYRGKHK ILVIAADERY
     LPTDNGKLFS TGNHPIETLL PLYHLHAAGF EFEVATISGL MTKFEYWAMP HKDEKVMPFF
     EQHKSLFRNP KKLADVVASL NADSEYAAIF VPGGHGALIG LPESQDVAAA LQWAIKNDRF
     VISLCHGPAA FLALRHSDNP LNGYSICAFP DAADKQTPDI GYMPGHLTWY FGEELKKMGM
     NIINDDITGR VHKDRKRLTG DSPFAANALG KLAAQEMLAA YAS
 
 
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