(data stored in SCRATCH zone)

SWISSPROT: C8U1S4_ECO10

ID   C8U1S4_ECO10            Unreviewed;       251 AA.
AC   C8U1S4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Hydroxyacylglutathione hydrolase {ECO:0000256|HAMAP-Rule:MF_01374};
DE            EC=3.1.2.6 {ECO:0000256|HAMAP-Rule:MF_01374};
DE   AltName: Full=Glyoxalase II {ECO:0000256|HAMAP-Rule:MF_01374};
DE            Short=Glx II {ECO:0000256|HAMAP-Rule:MF_01374};
GN   Name=gloB {ECO:0000256|HAMAP-Rule:MF_01374,
GN   ECO:0000313|EMBL:BAI29082.1};
GN   OrderedLocusNames=ECO103_0206 {ECO:0000313|EMBL:BAI29082.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29082.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29082.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-
CC       lactoyl-glutathione to form glutathione and D-lactic acid.
CC       {ECO:0000256|HAMAP-Rule:MF_01374, ECO:0000256|SAAS:SAAS01079168}.
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:0000256|HAMAP-Rule:MF_01374,
CC         ECO:0000256|SAAS:SAAS01116303};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01374};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01374};
CC   -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
CC       degradation; (R)-lactate from methylglyoxal: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01374, ECO:0000256|SAAS:SAAS01079155}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01374}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       Glyoxalase II family. {ECO:0000256|HAMAP-Rule:MF_01374,
CC       ECO:0000256|SAAS:SAAS01079161}.
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DR   EMBL; AP010958; BAI29082.1; -; Genomic_DNA.
DR   RefSeq; WP_001052751.1; NC_013353.1.
DR   SMR; C8U1S4; -.
DR   EnsemblBacteria; BAI29082; BAI29082; ECO103_0206.
DR   KEGG; eoh:ECO103_0206; -.
DR   HOGENOM; HOG000058041; -.
DR   KO; K01069; -.
DR   OMA; NYIWLLQ; -.
DR   BioCyc; ECOL585395:ECO103_RS01080-MONOMER; -.
DR   UniPathway; UPA00619; UER00676.
DR   Proteomes; UP000000959; 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; C8U1S4.
DR   SWISS-2DPAGE; C8U1S4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01374,
KW   ECO:0000256|SAAS:SAAS01079153, ECO:0000313|EMBL:BAI29082.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01374,
KW   ECO:0000256|SAAS:SAAS01079140};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01374, ECO:0000256|SAAS:SAAS01079142}.
FT   DOMAIN       11    165       Lactamase_B. {ECO:0000259|SMART:SM00849}.
FT   METAL        53     53       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL        55     55       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL        57     57       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL        58     58       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL       110    110       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL       127    127       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL       127    127       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL       165    165       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
SQ   SEQUENCE   251 AA;  28450 MW;  D9772CF8AED4FD29 CRC64;
     MNLNSIPAFD DNYIWVLNDE AGRCLIVDPG DAEPVLNAIT ANNWQPEAIF LTHHHHDHVG
     GVKELVEKFP QIVVYGPQET QDKGTTQVVK DGETAFVLGH EFSVIATPGH TLGHICYFSK
     PYLFCGDTLF SGGCGRLFEG TASQMYQSLN KLSALPDDTL VCCAHEYTLS NMKFALSILP
     HDLSINDYYR KVKELRAKNQ ITLPVILKNE RQINVFLRTE DIDLINVINE ETLLQQPEER
     FAWLRSKKDR F
//

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