ID   GHRA_YERE8              Reviewed;         313 AA.
AC   A1JRR3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase A;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
DE   AltName: Full=2-ketoacid reductase;
GN   Name=ghrA; OrderedLocusNames=YE2422;
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   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GhrA subfamily.
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DR   EMBL; AM286415; CAL12470.1; -; Genomic_DNA.
DR   RefSeq; YP_001006636.1; -.
DR   GeneID; 4714839; -.
DR   GenomeReviews; AM286415_GR; YE2422.
DR   KEGG; yen:YE2422; -.
DR   NMPDR; fig|630.2.peg.2347; -.
DR   OMA; A1JRR3; YALVWRA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:HAMAP.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IEA:HAMAP.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01666; -; 1.
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; PF02826; 2-Hacid_dh_C; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; FALSE_NEG.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; FALSE_NEG.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    313       Glyoxylate/hydroxypyruvate reductase A.
FT                                /FTId=PRO_0000348378.
FT   ACT_SITE    228    228       By similarity.
FT   ACT_SITE    276    276       Proton donor (By similarity).
SQ   SEQUENCE   313 AA;  34854 MW;  29D79951FB1E61DD CRC64;
     MNIIFYHPFF EAKQWLSGLQ SRLPTANIRQ WRRGDTQPAD YALVWQPPQE MLASRVELKG
     VFALGAGVDA ILDQERRHPG TLPAGVPLVR LEDTGMSLQM QEYVVATVLR YFRRMDEYQL
     QQQQKLWQPL EPHQHDKFTI GILGAGVLGK SVAHKLAEFG FTVRCWSRTP KQIDGVTSFA
     GQEKLPAFIQ GTQLLINLLP HTPQTAGILN QSLFSQLNAN AYIINIARGA HLLERDLLAA
     MNAGQVAAAT LDVFAEEPLP SMHPFWSHPR VTITPHIAAV TLPEVAMDQV VANIQAMEAG
     REPVGLVDVV RGY
//