ID GHRB_CITK8 Reviewed; 324 AA. AC A8ARD9; 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=CKO_05009; OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=290338; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., RA Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (AUG-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; CP000822; ABV16052.1; -; Genomic_DNA. DR RefSeq; YP_001456488.1; -. DR GeneID; 5580664; -. DR GenomeReviews; CP000822_GR; CKO_05009. DR KEGG; cko:CKO_05009; -. DR OMA; A8ARD9; 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_0000348379. 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; 35177 MW; DE6E2380C2B09A2B CRC64; MKPSIILYKA LPDDLLHRLE EHFTVTQVPN LRPETVEQHA QAFASAEGLL GSSETVNSAL LEKMPKLRAA STVSVGYDNF DVAALNARSV LLMHTPTVLT ETVADTVMAL VLSTARRVVE VAERVKVGEW TKSIGPDWFG TDVHHKTLGI VGMGRIGLAL AQRAHFGFNM PILYNARRHH PEAEERFNAR YCDLDTLLQA ADFVCLILPL TEETHHLFGA AQFAKMKSSA IFINAGRGPV VDETALIAAL QSGEIHAAGL DVFEQEPLPV DSPLLSLPNV VALPHIGSAT HETRYNMAAC AVDNLIDALQ GKVEKNCVNP QVAG //