ID GHRB_SALPB Reviewed; 324 AA.
AC A9MUT4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 29-MAY-2013, entry version 41.
DE RecName: Full=Glyoxylate/hydroxypyruvate reductase B;
DE EC=1.1.1.79;
DE EC=1.1.1.81;
GN Name=ghrB; OrderedLocusNames=SPAB_04530;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V.,
RA Nash W., Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-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 (By similarity).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. GhrB subfamily.
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DR EMBL; CP000886; ABX69843.1; -; Genomic_DNA.
DR RefSeq; YP_001590677.1; NC_010102.1.
DR ProteinModelPortal; A9MUT4; -.
DR STRING; 272994.SPAB_04530; -.
DR EnsemblBacteria; ABX69843; ABX69843; SPAB_04530.
DR GeneID; 5779691; -.
DR KEGG; spq:SPAB_04530; -.
DR PATRIC; 18535678; VBISalEnt120821_3668.
DR eggNOG; COG1052; -.
DR HOGENOM; HOG000136700; -.
DR KO; K00090; -.
DR OMA; FGMDVHH; -.
DR ProtClustDB; PRK15409; -.
DR BioCyc; SENT28901:GH9O-4520-MONOMER; -.
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 binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; -; 2.
DR HAMAP; MF_01667; 2-Hacid_dh_C_GhrB; 1; -.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR InterPro; IPR023756; Glyo/OHPyrv_Rdtase_B.
DR InterPro; IPR016040; NAD(P)-bd_dom.
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_0000348395.
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; 35412 MW; 28EC6CF78C19077B CRC64;
MKPSIILYKT LPDDLLHRLE AHFTVTQVPN LHPETVARHA QAFASAQGLL GTSETVNRAL
LEKMPALRAA STISVGYDNV EVDALTARKI VLMHTPTVLT ETVADTVMAL MLATARRVVD
VAERVKAGEW TESIGPAWFG VDVHHKTLGI VGMGRIGMAL AQRAHFGFTM PVLYHARRRH
QEAEDRFNAR YCDLDTLLQE ADFVCVILPL TTETRHLFGT TQFARMKSSA IFINAGRGPV
VDENALIAAL QNGEIYAAGL DVFEHEPLSV DSPLLNMSNV VAVPHIGSAT HETRYNMMAC
AVDNLIDALQ GKIEKNCVNP QAAG
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