(data stored in ACNUC7421 zone)

SWISSPROT: D4YXT0_SPHJU

ID   D4YXT0_SPHJU            Unreviewed;       240 AA.
AC   D4YXT0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 51.
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:BAI95162.1};
GN   OrderedLocusNames=SJA_C1-03280 {ECO:0000313|EMBL:BAI95162.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95162.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95162.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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:SAAS00846131}.
CC   -!- CATALYTIC ACTIVITY: S-(2-hydroxyacyl)glutathione + H(2)O =
CC       glutathione + a 2-hydroxy carboxylate. {ECO:0000256|HAMAP-
CC       Rule:MF_01374, ECO:0000256|SAAS:SAAS00846141}.
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:SAAS00846165}.
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:SAAS00846159}.
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DR   EMBL; AP010803; BAI95162.1; -; Genomic_DNA.
DR   RefSeq; WP_007686930.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-03280; -.
DR   EnsemblBacteria; BAI95162; BAI95162; SJA_C1-03280.
DR   GeneID; 29272030; -.
DR   KEGG; sjp:SJA_C1-03280; -.
DR   eggNOG; ENOG4108JMX; Bacteria.
DR   eggNOG; ENOG4111FEZ; LUCA.
DR   HOGENOM; HOG000058041; -.
DR   KO; K01069; -.
DR   OMA; NYIWLLQ; -.
DR   OrthoDB; POG091H03YM; -.
DR   UniPathway; UPA00619; UER00676.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-HAMAP.
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; D4YXT0.
DR   SWISS-2DPAGE; D4YXT0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01374,
KW   ECO:0000256|SAAS:SAAS00846130, ECO:0000313|EMBL:BAI95162.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01374,
KW   ECO:0000256|SAAS:SAAS00846147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01374, ECO:0000256|SAAS:SAAS00846150}.
FT   DOMAIN       12    170       Lactamase_B. {ECO:0000259|SMART:SM00849}.
FT   METAL        55     55       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL        57     57       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL        59     59       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL        60     60       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL       113    113       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL       132    132       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL       132    132       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
FT   METAL       170    170       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01374}.
SQ   SEQUENCE   240 AA;  25849 MW;  C655F8B172C95A7B CRC64;
     MLEVVRIPVL SDNYVWLLHD DASGETVAVD PAVAEPVLEA ARQRDWTISQ IWNTHWHGDH
     VGGNAAIKAA TGCTITGPAA EAEKIGTLDR MVREGDSVRI GAHQAAVLEV PAHTAGHVAY
     HLADDRLIFV GDTLFAMGCG RLFEGTAAQM FANMRRFAAL PDDTVVYCAH EYTQSNGRFA
     LTVEPDNAAL RARMAEVDAA RSRGEATVPT SVGQERATNV FMRASDVAQL AERRAAKDAA
//

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