ID GHRB_ENTS8 Reviewed; 324 AA. AC A7MKR1; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 02-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=ESA_04175; OS Enterobacter sakazakii (strain ATCC BAA-894). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., RA Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (JUL-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. 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; CP000783; ABU79356.1; -; Genomic_DNA. DR RefSeq; YP_001440192.1; -. DR GeneID; 5550656; -. DR GenomeReviews; CP000783_GR; ESA_04175. DR KEGG; esa:ESA_04175; -. DR OMA; A7MKR1; 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; 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_0000348380. 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; 35164 MW; 2F02C5A38C0F909B CRC64; MKPSVILYKS LPDDLLARLE SHFNVTRVPD LSPETIEAHA SAFSEAQGLL GSSEKVDAAL LEKMPALRAA STVSVGYDNF DVDALSAKKI ALMHTPTVLT ETVADTLMTL VLTTARRALE VAERVKAGEW TGSIGPDWFG CDVHHKTLGI VGMGRIGLAL AQRAHFGFNM PILYNARRHH SEAEERFNAR YCDLDTLLAE SDFVCVILPL TDETHHMIGA EQFRKMKKSA IFINAGRGPV VDENALIAAL QSGEIHAAGL DVFEQEPLSK DSPLLTMKNV VALPHIGSAT HETRYNMAAC AVDNLINALN GDVSQNCVNP KAVK //