ID   GHRB_ENT38              Reviewed;         324 AA.
AC   A4W577;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase B;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
GN   Name=ghrB; OrderedLocusNames=Ent638_0167;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Enterobacter sp. 638.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000653; ABP58857.1; -; Genomic_DNA.
DR   RefSeq; YP_001174908.1; -.
DR   GeneID; 5113265; -.
DR   GenomeReviews; CP000653_GR; Ent638_0167.
DR   KEGG; ent:Ent638_0167; -.
DR   NMPDR; fig|399742.4.peg.248; -.
DR   OMA; A4W577; MARCAVE.
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; 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    324       Glyoxylate/hydroxypyruvate reductase B.
FT                                /FTId=PRO_0000348381.
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;  35661 MW;  1323B43A8356FC68 CRC64;
     MKPSVILYKT LPDDLQKRLE EHFTVTQMKN LNPETVAEHA DAFASAAGLL GSSEKVDTAL
     LEKMPKLRAT STISVGYDNF DVDALNTRKI LLMHTPYALT ETVADTLMAL VLSTARRVVE
     VAERVKAGEW TKSIGPDWFG VDVHGKTLGI VGMGRIGLAL AQRAHFGFNM PILYNARRHH
     SEAEERFEAR YCELETLLQE ADYVCLILPL TDETHHLIGK AEFEKMKKSA IFINAGRGPV
     VDEKALIEAL QKGEIHAAGL DVFEQEPLPV DSPLLTMSNV VSLPHIGSAT HETRYNMAAT
     AVDNLINALN GNVEKNCVNP HVNA
//