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Database: UniProt
Entry: P58220
LinkDB: P58220
Original site: P58220 
ID   GHRB_ECO57              Reviewed;         324 AA.
AC   P58220;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 1.
DT   05-DEC-2018, entry version 115.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase B;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
GN   Name=tkrA; OrderedLocusNames=Z4978, ECs4438;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate
CC       and hydroxypyruvate into glycolate and glycerate, respectively.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycolate + NADP(+) = glyoxylate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:10992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.79;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH;
CC         Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC         ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.81;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16659, ChEBI:CHEBI:17180, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.81;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GhrB subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG58702.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB37861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE005174; AAG58702.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB37861.1; ALT_INIT; Genomic_DNA.
DR   PIR; B86030; B86030.
DR   PIR; F91183; F91183.
DR   RefSeq; NP_312465.2; NC_002695.1.
DR   RefSeq; WP_000805027.1; NZ_NOKN01000002.1.
DR   ProteinModelPortal; P58220; -.
DR   SMR; P58220; -.
DR   STRING; 155864.Z4978; -.
DR   EnsemblBacteria; AAG58702; AAG58702; Z4978.
DR   EnsemblBacteria; BAB37861; BAB37861; BAB37861.
DR   GeneID; 915671; -.
DR   KEGG; ece:Z4978; -.
DR   KEGG; ecs:ECs4438; -.
DR   PATRIC; fig|386585.9.peg.4645; -.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   KO; K00090; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   HAMAP; MF_01667; 2_Hacid_dh_C_GhrB; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR023756; Glyo/OHPyrv_Rdtase_B.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 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;
KW   Reference proteome.
FT   CHAIN         1    324       Glyoxylate/hydroxypyruvate reductase B.
FT                                /FTId=PRO_0000076030.
FT   ACT_SITE    237    237       {ECO:0000250}.
FT   ACT_SITE    266    266       {ECO:0000250}.
FT   ACT_SITE    285    285       Proton donor. {ECO:0000250}.
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
//
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