ID GHRB_SHIB3 Reviewed; 324 AA. AC B2U573; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 16-JUN-2009, entry version 8. DE RecName: Full=Glyoxylate/hydroxypyruvate reductase B; DE EC=1.1.1.79; DE EC=1.1.1.81; GN Name=ghrB; OrderedLocusNames=SbBS512_E3973; OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=344609; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R., RA Jiang L., Ravel J., Sebastian Y.; RT "Complete sequence of Shigella boydii serotype 18 strain BS512."; RL Submitted (MAY-2008) 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; CP001063; ACD06290.1; -; Genomic_DNA. DR RefSeq; YP_001882254.1; -. DR GeneID; 6270543; -. DR GenomeReviews; CP001063_GR; SbBS512_E3973. DR KEGG; sbc:SbBS512_E3973; -. DR OMA; B2U573; 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_0000348399. 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 //