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Database: UniProt
Entry: P37666
LinkDB: P37666
Original site: P37666 
ID   GHRB_ECOLI              Reviewed;         324 AA.
AC   P37666; Q2M7L4;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 3.
DT   13-FEB-2019, entry version 158.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase B;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
DE   AltName: Full=2-ketoaldonate reductase;
DE   AltName: Full=2-ketogluconate reductase;
DE            Short=2KR;
DE            EC=1.1.1.215;
GN   Name=ghrB; Synonyms=tkrA, yiaE; OrderedLocusNames=b3553, JW5656;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the
RT   region from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
RP   TO C-TERMINUS.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-22, SUBUNIT, SUBSTRATE SPECIFICITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9811658;
RA   Yum D.-Y., Lee B.-Y., Hahm D.-H., Pan J.-G.;
RT   "The yiaE gene, located at 80.1 minutes on the Escherichia coli
RT   chromosome, encodes a 2-ketoaldonate reductase.";
RL   J. Bacteriol. 180:5984-5988(1998).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-8.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded
RT   in the genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [6]
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=11237876; DOI=10.1042/0264-6021:3540707;
RA   Nunez M.F., Pellicer M.T., Badia J., Aguilar J., Baldoma L.;
RT   "Biochemical characterization of the 2-ketoacid reductases encoded by
RT   ycdW and yiaE genes in Escherichia coli.";
RL   Biochem. J. 354:707-715(2001).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate
CC       and hydroxypyruvate into glycolate and glycerate, respectively.
CC       Can also reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D-
CC       gluconate (5KDG), 2-keto-D-gluconate (2KDG) to D-gluconate, and 2-
CC       keto-L-gulonate (2KLG) to L-idonate (IA), but it is not its
CC       physiological function. Inactive towards 2-oxoglutarate,
CC       oxaloacetate, pyruvate, 5-keto-D-gluconate, D-fructose and L-
CC       sorbose. Activity with NAD is very low.
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; Evidence={ECO:0000269|PubMed:11237876};
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; Evidence={ECO:0000269|PubMed:11237876};
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         Evidence={ECO:0000269|PubMed:11237876};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-gluconate + NADP(+) = 2-dehydro-D-gluconate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:16653, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16808, ChEBI:CHEBI:18391, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.215;
CC         Evidence={ECO:0000269|PubMed:11237876};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.7 mM for hydroxypyruvate (at pH 7.5)
CC         {ECO:0000269|PubMed:11237876, ECO:0000269|PubMed:9811658};
CC         KM=1.5 mM for 2-oxo-D-gluconate (at pH 7.5)
CC         {ECO:0000269|PubMed:11237876, ECO:0000269|PubMed:9811658};
CC         KM=6.6 mM for glyoxylate (at pH 7.5)
CC         {ECO:0000269|PubMed:11237876, ECO:0000269|PubMed:9811658};
CC         Vmax=345 umol/min/mg enzyme with glyoxylate as substrate (at pH
CC         7) {ECO:0000269|PubMed:11237876, ECO:0000269|PubMed:9811658};
CC         Vmax=123 umol/min/mg enzyme with hydroxypyruvate as substrate
CC         (at pH 7) {ECO:0000269|PubMed:11237876,
CC         ECO:0000269|PubMed:9811658};
CC         Vmax=69 umol/min/mg enzyme with 2-oxo-D-gluconate as substrate
CC         (at pH 7) {ECO:0000269|PubMed:11237876,
CC         ECO:0000269|PubMed:9811658};
CC         Note=The catalytic efficiency is better for hydroxypyruvate than
CC         glyoxylate with NADPH as electron donor.;
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:11237876,
CC         ECO:0000269|PubMed:9811658};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9811658}.
CC   -!- INTERACTION:
CC       P36938:pgm; NbExp=2; IntAct=EBI-562547, EBI-542427;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Constitutively expressed.
CC       {ECO:0000269|PubMed:11237876}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GhrB subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB18530.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAB18530.1; Type=Frameshift; Positions=324; Evidence={ECO:0000305};
DR   EMBL; U00039; AAB18530.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; AAC76577.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77742.1; -; Genomic_DNA.
DR   PIR; C65154; C65154.
DR   RefSeq; NP_418009.2; NC_000913.3.
DR   RefSeq; WP_000805038.1; NZ_LN832404.1.
DR   ProteinModelPortal; P37666; -.
DR   SMR; P37666; -.
DR   BioGrid; 4259301; 35.
DR   DIP; DIP-10997N; -.
DR   IntAct; P37666; 1.
DR   STRING; 316385.ECDH10B_3732; -.
DR   EPD; P37666; -.
DR   jPOST; P37666; -.
DR   PaxDb; P37666; -.
DR   PRIDE; P37666; -.
DR   EnsemblBacteria; AAC76577; AAC76577; b3553.
DR   EnsemblBacteria; BAE77742; BAE77742; BAE77742.
DR   GeneID; 948074; -.
DR   KEGG; ecj:JW5656; -.
DR   KEGG; eco:b3553; -.
DR   PATRIC; fig|1411691.4.peg.3161; -.
DR   EchoBASE; EB2181; -.
DR   EcoGene; EG12272; ghrB.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   InParanoid; P37666; -.
DR   KO; K00090; -.
DR   PhylomeDB; P37666; -.
DR   BioCyc; EcoCyc:MONOMER-43; -.
DR   BioCyc; ECOL316407:JW5656-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-43; -.
DR   SABIO-RK; P37666; -.
DR   PRO; PR:P37666; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008873; F:gluconate 2-dehydrogenase activity; IDA:EcoCyc.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IDA:EcoCyc.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046181; P:ketogluconate catabolic process; IMP:EcoCyc.
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   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Gluconate utilization; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN         1    324       Glyoxylate/hydroxypyruvate reductase B.
FT                                /FTId=PRO_0000076029.
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;  1B21339B1337D255 CRC64;
     MKPSVILYKA LPDDLLQRLQ EHFTVHQVAN LSPQTVEQNA AIFAEAEGLL GSNENVNAAL
     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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