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Database: UniProt
Entry: B2VCD1
LinkDB: B2VCD1
Original site: B2VCD1 
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   01-OCT-2014, entry version 46.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase B {ECO:0000255|HAMAP-Rule:MF_01667};
DE            EC=1.1.1.79 {ECO:0000255|HAMAP-Rule:MF_01667};
DE            EC=1.1.1.81 {ECO:0000255|HAMAP-Rule:MF_01667};
GN   Name=ghrB {ECO:0000255|HAMAP-Rule:MF_01667};
GN   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.
CC       {ECO:0000255|HAMAP-Rule:MF_01667}.
CC   -!- CATALYTIC ACTIVITY: Glycolate + NADP(+) = glyoxylate + NADPH.
CC       {ECO:0000255|HAMAP-Rule:MF_01667}.
CC   -!- CATALYTIC ACTIVITY: D-glycerate + NAD(P)(+) = hydroxypyruvate +
CC       NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_01667}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01667}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01667}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GhrB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01667}.
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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; MLAQAGP; -.
DR   OrthoDB; EOG6VXFC3; -.
DR   BioCyc; ETAS465817:GI36-3549-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_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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    321       Glyoxylate/hydroxypyruvate reductase B.
FT                                /FTId=PRO_1000187291.
FT   ACT_SITE    237    237       {ECO:0000255|HAMAP-Rule:MF_01667}.
FT   ACT_SITE    266    266       {ECO:0000255|HAMAP-Rule:MF_01667}.
FT   ACT_SITE    285    285       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01667}.
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
//
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