ID GHRB_ERWT9 Reviewed; 321 AA.
AC B2VCD1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 29-MAY-2013, entry version 39.
DE RecName: Full=Glyoxylate/hydroxypyruvate reductase B;
DE EC=1.1.1.79;
DE EC=1.1.1.81;
GN Name=ghrB; OrderedLocusNames=ETA_34410;
OS Erwinia tasmaniensis (strain DSM 17950 / Et1/99).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Erwinia.
OX NCBI_TaxID=338565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / Et1/99;
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO98487.1; -; Genomic_DNA.
DR RefSeq; YP_001909347.1; NC_010694.1.
DR ProteinModelPortal; B2VCD1; -.
DR STRING; 465817.ETA_34410; -.
DR EnsemblBacteria; CAO98487; CAO98487; ETA_34410.
DR GeneID; 6298409; -.
DR KEGG; eta:ETA_34410; -.
DR PATRIC; 20432811; VBIErwTas9546_3532.
DR eggNOG; COG1052; -.
DR HOGENOM; HOG000136700; -.
DR KO; K00090; -.
DR OMA; ERSMKPS; -.
DR ProtClustDB; PRK15409; -.
DR BioCyc; ETAS465817:GI36-3549-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; FALSE_NEG.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.
FT CHAIN 1 321 Glyoxylate/hydroxypyruvate reductase B.
FT /FTId=PRO_1000187291.
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 321 AA; 35117 MW; 9BE94B1F2E0B6FB4 CRC64;
MKPSVVLYKS LPEDLRARLD EHCHVTEING LTAENIAKHE DVFRQAEGIL GSGGKVDAEF
LRQAPKLRVA SSISVGYDNF DVAALNDRGV LLMHTPTVLT ETVADTMMAL VLSSARRVVE
MAERVKSGEW RGSISSDWFG IDVHHKKLGI LGMGRIGLAL AQRAHLGFGM PILYNARKHH
DEAEQRFDAE YCDLDTLLAE SDFLCISLPL TEQTHHLIGR EQLAKMKRSA ILINAGRGPV
VDEQALIAAL KDGTLHAAGL DVFEQEPLPV SSELLALRNV VALPHIGSAT HETRYGMAKD
AVDNLIAALN GKVEKNCVNP R
//
