ID   GHRB_ECOSM              Reviewed;         324 AA.
AC   B1LJB3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 10.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase B;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
GN   Name=ghrB; OrderedLocusNames=EcSMS35_3874;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18708504; DOI=10.1128/JB.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia
RT   coli SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000970; ACB16053.1; -; Genomic_DNA.
DR   RefSeq; YP_001745839.1; -.
DR   GeneID; 6145008; -.
DR   GenomeReviews; CP000970_GR; EcSMS35_3874.
DR   KEGG; ecm:EcSMS35_3874; -.
DR   OMA; B1LJB3; 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_0000348385.
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;  35387 MW;  26A5ACFD218B903A CRC64;
     MKPSVILYKA LPDDLLQRLQ EHFTVHQVAN LSPQTVEQNA AIFAEAEGLL GSNENVDAAL
     LEKMPKLRAT STISVGYDNF DVDALTARKI LLMHTPTVLT ETVADTLMAL VLSTARRVVE
     VAERVKAGEW TASIGPDWYG TDVHHKTLGI VGMGRIGMAL AQRAQFGFNM PILYNARRHH
     KEAEERFNAR YCDLDTLLQE SDFVCLILPL TDETHHLFGA EQFAKMKSSA IFINAGRGPV
     VDENALIAAL QKGEIHAAGL DVFEQEPLSV DSPLLSMANV VAVPHIGSAT HETRYGMAAC
     AVDNLIDALQ GKVEKNCVNP HVAD
//