(data stored in ACNUC7421 zone)

SWISSPROT: GLO2_ECO27

ID   GLO2_ECO27              Reviewed;         251 AA.
AC   B7UJA8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Hydroxyacylglutathione hydrolase {ECO:0000255|HAMAP-Rule:MF_01374};
DE            EC=3.1.2.6 {ECO:0000255|HAMAP-Rule:MF_01374};
DE   AltName: Full=Glyoxalase II {ECO:0000255|HAMAP-Rule:MF_01374};
DE            Short=Glx II {ECO:0000255|HAMAP-Rule:MF_01374};
GN   Name=gloB {ECO:0000255|HAMAP-Rule:MF_01374};
GN   OrderedLocusNames=E2348C_0212;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-
CC       lactoyl-glutathione to form glutathione and D-lactic acid.
CC       {ECO:0000255|HAMAP-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
CC       degradation; (R)-lactate from methylglyoxal: step 2/2.
CC       {ECO:0000255|HAMAP-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; FM180568; CAS07760.1; -; Genomic_DNA.
DR   RefSeq; WP_001052743.1; NC_011601.1.
DR   SMR; B7UJA8; -.
DR   EnsemblBacteria; CAS07760; CAS07760; E2348C_0212.
DR   KEGG; ecg:E2348C_0212; -.
DR   KO; K01069; -.
DR   OMA; NYIWLLQ; -.
DR   BioCyc; ECOL574521:E2348C_RS01120-MONOMER; -.
DR   UniPathway; UPA00619; UER00676.
DR   Proteomes; UP000008205; Chromosome.
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_hydrola; 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   PIRSF; PIRSF005457; Glx; 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; B7UJA8.
DR   SWISS-2DPAGE; B7UJA8.
KW   Complete proteome; Hydrolase; Metal-binding; Zinc.
FT   CHAIN         1    251       Hydroxyacylglutathione hydrolase.
FT                                /FTId=PRO_1000184177.
FT   METAL        53     53       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL        55     55       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL        57     57       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL        58     58       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL       110    110       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL       127    127       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL       127    127       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL       165    165       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
SQ   SEQUENCE   251 AA;  28476 MW;  B519BF5C36928B5A CRC64;
     MNLNSIPAFD DNYIWVLNDE AGRCLIVDPG DAEPVLNAIS ANNWQPEAIF LTHHHHDHVG
     GVKELVEKFP QIVVYGPQET QDKGTTQVVK DGETAFVLGH EFSVIATPGH TLGHICYFSK
     PYLFCGDTLF SGGCGRLFEG TPSQMYQSLK KLSALPDDTL VCCAHEYTLS NMKFALSILP
     HDLSINDYYR KVKELRAKNQ ITLPVILKNE RQINVFLRTE DIDLINVINE ETLLQQPEER
     FAWLRSKKDR F
//

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