ID   GHRB_ECO24              Reviewed;         324 AA.
AC   A7ZTA0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 13.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase B;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
GN   Name=ghrB; OrderedLocusNames=EcE24377A_4049;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV17627.1; -; Genomic_DNA.
DR   RefSeq; YP_001465029.1; -.
DR   GeneID; 5590663; -.
DR   GenomeReviews; CP000800_GR; EcE24377A_4049.
DR   KEGG; ecw:EcE24377A_4049; -.
DR   OMA; A7ZTA0; 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; FALSE_NEG.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    324       Glyoxylate/hydroxypyruvate reductase B.
FT                                /FTId=PRO_0000348387.
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   324 AA;  35396 MW;  A6EB3399119DD250 CRC64;
     MKPSVILYKA LPDDLLQRLQ EHFTVHQVAN LSPQTVEQNA AIFAEAEGLL GSNENVDAAL
     LEKMPKLRAT STISVGYDNF DVDALTARKI LLMHTPTVLT ETVADTLMAL VLSTARRVVE
     VAERVKAGEW TASIGPDWYG TDVHHKTLGI VGMGRIGMAL AQRAHFGFNM PILYNARRHH
     KEAEERFNAR YCDLDTLLQE SDFVCLILPL TDETHHLFGA EQFAKMKSSA IFINAGRGPV
     VDENALIAAL QKGEIHAAGL DVFEQEPLSV DSPLLSMANV VAVPHIGSAT HETRYGMAAC
     AVDNLIDALQ GKVEKNCVNP HVAD
//