(data stored in ACNUC7421 zone)

SWISSPROT: GLO2_ECODH

ID   GLO2_ECODH              Reviewed;         251 AA.
AC   B1XD76;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   30-AUG-2017, entry version 60.
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=ECDH10B_0193;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB01385.1; -; Genomic_DNA.
DR   RefSeq; WP_001052715.1; NC_010473.1.
DR   ProteinModelPortal; B1XD76; -.
DR   SMR; B1XD76; -.
DR   EnsemblBacteria; ACB01385; ACB01385; ECDH10B_0193.
DR   KEGG; ecd:ECDH10B_0193; -.
DR   eggNOG; ENOG4108RW0; Bacteria.
DR   eggNOG; COG0491; LUCA.
DR   HOGENOM; HOG000058041; -.
DR   KO; K01069; -.
DR   OMA; NYIWLLQ; -.
DR   UniPathway; UPA00619; UER00676.
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; B1XD76.
DR   SWISS-2DPAGE; B1XD76.
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN         1    251       Hydroxyacylglutathione hydrolase.
FT                                /FTId=PRO_1000144762.
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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