位置:首页 > 蛋白库 > HCHA_STAA8
HCHA_STAA8
ID   HCHA_STAA8              Reviewed;         292 AA.
AC   Q2G0M7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=SAOUHSC_00533;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000253; ABD29681.1; -; Genomic_DNA.
DR   RefSeq; WP_000076404.1; NZ_LS483365.1.
DR   RefSeq; YP_499105.1; NC_007795.1.
DR   PDB; 5XR2; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-292.
DR   PDB; 5XR3; X-ray; 3.01 A; A/B/C/D/E/F/G/H=1-292.
DR   PDBsum; 5XR2; -.
DR   PDBsum; 5XR3; -.
DR   AlphaFoldDB; Q2G0M7; -.
DR   SMR; Q2G0M7; -.
DR   STRING; 1280.SAXN108_0605; -.
DR   MEROPS; C56.006; -.
DR   EnsemblBacteria; ABD29681; ABD29681; SAOUHSC_00533.
DR   GeneID; 3920386; -.
DR   KEGG; sao:SAOUHSC_00533; -.
DR   PATRIC; fig|93061.5.peg.479; -.
DR   eggNOG; COG0693; Bacteria.
DR   HOGENOM; CLU_066933_0_0_9; -.
DR   OMA; GEKTGFW; -.
DR   PRO; PR:Q2G0M7; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0019172; F:glyoxalase III activity; IBA:GO_Central.
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:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA damage; DNA repair; Hydrolase;
KW   Reference proteome; Stress response.
FT   CHAIN           1..292
FT                   /note="Protein/nucleic acid deglycase HchA"
FT                   /id="PRO_1000064284"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024