ID   GHRB_YERE8              Reviewed;         326 AA.
AC   A1JT62;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase B;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
GN   Name=ghrB; OrderedLocusNames=YE4159;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the
RT   high pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate
CC       and hydroxypyruvate into glycolate and glycerate, respectively (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Glycolate + NADP(+) = glyoxylate + NADPH.
CC   -!- CATALYTIC ACTIVITY: D-glycerate + NAD(P)(+) = hydroxypyruvate +
CC       NAD(P)H.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GhrB subfamily.
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DR   EMBL; AM286415; CAL14175.1; -; Genomic_DNA.
DR   RefSeq; YP_001008293.1; -.
DR   GeneID; 4716553; -.
DR   GenomeReviews; AM286415_GR; YE4159.
DR   KEGG; yen:YE4159; -.
DR   NMPDR; fig|630.2.peg.4084; -.
DR   OMA; A1JT62; KVYIAEP.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:HAMAP.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IEA:HAMAP.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:HAMAP.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01667; -; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH.
DR   InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; FALSE_NEG.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    326       Glyoxylate/hydroxypyruvate reductase B.
FT                                /FTId=PRO_0000348405.
FT   ACT_SITE    237    237       By similarity.
FT   ACT_SITE    266    266       By similarity.
FT   ACT_SITE    285    285       Proton donor (By similarity).
SQ   SEQUENCE   326 AA;  35256 MW;  44D7E34E4330849E CRC64;
     MKPSIVLYKS IPADLHQRLE QHFTVNSFEG LSSDNQPELL SALQQAEGLI GSGGKIDQAF
     LERAPKLRAA STISVGYDNF DVDALSQRGI ALMHTPTVLT ETVADTMMAL VLSSARRVVE
     LAERVKAGEW QDSIGDDWFG VDVHHKTIGI LGMGRIGMAL AQRAHFGFSM PVLYTSRRPH
     EAAEKRFGAR RCSLDTLLAE VDFLCITLPM TEQTYHMIGP EQLAKMKSSA ILINAGRGPV
     VDEQALIAAL QDGTIHAAGL DVFAQEPLPV ESPLLKLPNV VAVPHIGSAT HETRYNMAAC
     AVDNLIAALT GTVTENCVNP QVLQQA
//