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Database: UniProt
Entry: A9MUT4
LinkDB: A9MUT4
Original site: A9MUT4 
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   14-MAY-2014, entry version 46.
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   PATRIC; 18535678; VBISalEnt120821_3668.
DR   eggNOG; COG1052; -.
DR   HOGENOM; HOG000136700; -.
DR   OMA; SGEIHAA; -.
DR   OrthoDB; EOG6VXFC3; -.
DR   BioCyc; SENT28901:GH9O-4520-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-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; 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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