(data stored in ACNUC7421 zone)

SWISSPROT: GLO2_METNO

ID   GLO2_METNO              Reviewed;         255 AA.
AC   B8ICA2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   30-AUG-2017, entry version 56.
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=Mnod_0448;
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001349; ACL55490.1; -; Genomic_DNA.
DR   RefSeq; WP_015927201.1; NC_011894.1.
DR   ProteinModelPortal; B8ICA2; -.
DR   SMR; B8ICA2; -.
DR   STRING; 460265.Mnod_0448; -.
DR   EnsemblBacteria; ACL55490; ACL55490; Mnod_0448.
DR   KEGG; mno:Mnod_0448; -.
DR   eggNOG; ENOG4108JMX; Bacteria.
DR   eggNOG; ENOG4111FEZ; LUCA.
DR   HOGENOM; HOG000058041; -.
DR   KO; K01069; -.
DR   OMA; HTVGHMI; -.
DR   OrthoDB; POG091H03YM; -.
DR   UniPathway; UPA00619; UER00676.
DR   Proteomes; UP000008207; 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; B8ICA2.
DR   SWISS-2DPAGE; B8ICA2.
KW   Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN         1    255       Hydroxyacylglutathione hydrolase.
FT                                /FTId=PRO_1000184181.
FT   METAL        55     55       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL        57     57       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL        59     59       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL        60     60       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL       113    113       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL       132    132       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL       132    132       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
FT   METAL       170    170       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01374}.
SQ   SEQUENCE   255 AA;  27842 MW;  62998CFEF830CD1E CRC64;
     MPEIRTFLCR SDNIGVLLHD PVTSACAAID VPEAGAVLRA LKETGWRLTD ILVTHRHFDH
     VEGIPEVKAR TGARVTAPAK AGDAVPEVDA TVREGDVVKV GSLVGTVWET PGHCADHVTY
     WFERERLAFA GDTLFTLGCG RVMESPPEVL WRSLSRFLAL PDETAIYSGH DYVLSNARFA
     LAADPDNSNL KARAELAERV KRDGRFLIPT TLGEEKATNP FLRAGEPALA RSVDMAPGSD
     PAAVFAALRE WKNRF
//

If you have problems or comments...

PBIL Back to PBIL home page