(data stored in ACNUC7421 zone)

SWISSPROT: GLO2_ECO57

ID   GLO2_ECO57              Reviewed;         251 AA.
AC   P0AC85; Q47677;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 79.
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=Z0236, ECs0208;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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: S-(2-hydroxyacyl)glutathione + H(2)O =
CC       glutathione + a 2-hydroxy carboxylate. {ECO:0000255|HAMAP-
CC       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; AE005174; AAG54508.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33631.1; -; Genomic_DNA.
DR   PIR; H85505; H85505.
DR   PIR; H90654; H90654.
DR   RefSeq; NP_308235.1; NC_002695.1.
DR   RefSeq; WP_001052715.1; NZ_MWVM01000070.1.
DR   ProteinModelPortal; P0AC85; -.
DR   SMR; P0AC85; -.
DR   STRING; 155864.Z0236; -.
DR   EnsemblBacteria; AAG54508; AAG54508; Z0236.
DR   EnsemblBacteria; BAB33631; BAB33631; BAB33631.
DR   GeneID; 914044; -.
DR   KEGG; ece:Z0236; -.
DR   KEGG; ecs:ECs0208; -.
DR   PATRIC; fig|386585.9.peg.312; -.
DR   eggNOG; ENOG4108RW0; Bacteria.
DR   eggNOG; COG0491; LUCA.
DR   HOGENOM; HOG000058041; -.
DR   KO; K01069; -.
DR   UniPathway; UPA00619; UER00676.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-EC.
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   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; P0AC85.
DR   SWISS-2DPAGE; P0AC85.
KW   Complete proteome; Hydrolase; Metal-binding; Zinc.
FT   CHAIN         1    251       Hydroxyacylglutathione hydrolase.
FT                                /FTId=PRO_0000192352.
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;  28434 MW;  D59948B6E12809F5 CRC64;
     MNLNSIPAFD DNYIWVLNDE AGRCLIVDPG DAEPVLNAIA ANNWQPEAIF LTHHHHDHVG
     GVKELVEKFP QIVVYGPQET QDKGTTQVVK DGETAFVLGH EFSVIATPGH TLGHICYFSK
     PYLFCGDTLF SGGCGRLFEG TASQMYQSLK KLSALPDDTL VCCAHEYTLS NMKFALSILP
     HDLSINDYYR KVKELRAKNQ ITLPVILKNE RQINVFLRTE DIDLINVINE ETLLQQPEER
     FAWLRSKKDR F
//

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