(data stored in SCRATCH3701 zone)

SWISSPROT: GLO21_VIBVY

ID   GLO21_VIBVY             Reviewed;         247 AA.
AC   Q7MQ55;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 93.
DE   RecName: Full=Hydroxyacylglutathione hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_01374};
DE            EC=3.1.2.6 {ECO:0000255|HAMAP-Rule:MF_01374};
DE   AltName: Full=Glyoxalase II 1 {ECO:0000255|HAMAP-Rule:MF_01374};
DE            Short=Glx II 1 {ECO:0000255|HAMAP-Rule:MF_01374};
GN   Name=gloB1 {ECO:0000255|HAMAP-Rule:MF_01374}; OrderedLocusNames=VV0153;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC       glutathione to form glutathione and D-lactic acid. {ECO:0000255|HAMAP-
CC       Rule:MF_01374}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy
CC         carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01374};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01374};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01374};
CC   -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC       (R)-lactate from methylglyoxal: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_01374}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01374}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       Glyoxalase II family. {ECO:0000255|HAMAP-Rule:MF_01374}.
DR   EMBL; BA000037; BAC92917.1; -; Genomic_DNA.
DR   RefSeq; WP_011149160.1; NC_005139.1.
DR   SMR; Q7MQ55; -.
DR   STRING; 672.VV93_v1c34970; -.
DR   EnsemblBacteria; BAC92917; BAC92917; BAC92917.
DR   GeneID; 2622912; -.
DR   KEGG; vvy:VV0153; -.
DR   HOGENOM; HOG000058041; -.
DR   KO; K01069; -.
DR   OMA; FAMLVEP; -.
DR   UniPathway; UPA00619; UER00676.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro.
DR   CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_01374; Glyoxalase_2; 1.
DR   InterPro; IPR035680; Clx_II_MBL.
DR   InterPro; IPR032282; HAGH_C.
DR   InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF16123; HAGH_C; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7MQ55.
DR   SWISS-2DPAGE; Q7MQ55.
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..247
FT                   /note="Hydroxyacylglutathione hydrolase 1"
FT                   /id="PRO_0000309724"
FT   METAL           54
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   METAL           56
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   METAL           58
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   METAL           59
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   METAL           111
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   METAL           128
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   METAL           128
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   METAL           165
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
SQ   SEQUENCE   247 AA;  28352 MW;  CE35A1A9430D9D80 CRC64;
     MSLSITHEKS LIDNYIWILF DKSKAIVIDP GESEKIINFL DKNNLTLEFI FLTHGHCDHT
     KGVFSLKEKF PNASLFVPIG LELGLGESII KEGDELNLLN STFNVLELPG HTDNHIGIMY
     KDNLFCGDVL FSAGCGRVGS NYKDMYLSLK KIKSMDDKTK IYFSHEYTLD NLKFAHYIDP
     KNKNIINYIE VFKEKPDTVS APTTLLLEKE INPFLRLSEN IDIKNKINNE FDAFVYLRKL
     KDKFNSI
//

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