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Database: UniProt
Entry: P75913
LinkDB: P75913
Original site: P75913 
ID   GHRA_ECOLI              Reviewed;         312 AA.
AC   P75913; Q9R3M8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   13-FEB-2019, entry version 136.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase A;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
DE   AltName: Full=2-ketoacid reductase;
GN   Name=ghrA; Synonyms=ycdW; OrderedLocusNames=b1033, JW5146;
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 1-10, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP   INDUCTION, SUBCELLULAR LOCATION, AND 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).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=B / BL21;
RX   PubMed=10493123;
RX   DOI=10.1002/(SICI)1522-2683(19990801)20:11<2181::AID-ELPS2181>3.0.CO;2-Q;
RA   Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT   "Enrichment of low abundance proteins of Escherichia coli by
RT   hydroxyapatite chromatography.";
RL   Electrophoresis 20:2181-2195(1999).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate
CC       and hydroxypyruvate into glycolate and glycerate, respectively.
CC       Inactive towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate
CC       and pyruvate. Only D- and L-glycerate are involved in the
CC       oxidative activity with NADP. 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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.6 mM for glyoxylate (at 25 degrees Celsius and pH 7)
CC         {ECO:0000269|PubMed:11237876};
CC         KM=1.0 mM for hydroxypyruvate (at 25 degrees Celsius and pH 7)
CC         {ECO:0000269|PubMed:11237876};
CC         Vmax=120 umol/min/mg enzyme with glyoxylate as substrate (at 25
CC         degrees Celsius and pH 7) {ECO:0000269|PubMed:11237876};
CC         Vmax=20 umol/min/mg enzyme with hydroxypyruvate as substrate (at
CC         25 degrees Celsius and pH 7) {ECO:0000269|PubMed:11237876};
CC         Note=The catalytic efficiency is better for glyoxylate than
CC         hydroxypyruvate with NADPH as electron donor.;
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:11237876};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11237876}.
CC   -!- INDUCTION: Constitutively expressed.
CC       {ECO:0000269|PubMed:11237876}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GhrA subfamily. {ECO:0000305}.
DR   EMBL; U00096; AAC74117.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35814.1; -; Genomic_DNA.
DR   PIR; F64845; F64845.
DR   RefSeq; NP_415551.2; NC_000913.3.
DR   RefSeq; WP_000351317.1; NZ_LN832404.1.
DR   ProteinModelPortal; P75913; -.
DR   SMR; P75913; -.
DR   BioGrid; 4260060; 17.
DR   IntAct; P75913; 1.
DR   STRING; 316385.ECDH10B_1105; -.
DR   EPD; P75913; -.
DR   jPOST; P75913; -.
DR   PaxDb; P75913; -.
DR   PRIDE; P75913; -.
DR   EnsemblBacteria; AAC74117; AAC74117; b1033.
DR   EnsemblBacteria; BAA35814; BAA35814; BAA35814.
DR   GeneID; 946431; -.
DR   KEGG; ecj:JW5146; -.
DR   KEGG; eco:b1033; -.
DR   PATRIC; fig|1411691.4.peg.1238; -.
DR   EchoBASE; EB3628; -.
DR   EcoGene; EG13869; ghrA.
DR   eggNOG; ENOG4105JPG; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136694; -.
DR   InParanoid; P75913; -.
DR   KO; K12972; -.
DR   PhylomeDB; P75913; -.
DR   BioCyc; EcoCyc:G6539-MONOMER; -.
DR   BioCyc; ECOL316407:JW5146-MONOMER; -.
DR   BioCyc; MetaCyc:G6539-MONOMER; -.
DR   SABIO-RK; P75913; -.
DR   PRO; PR:P75913; -.
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:0030267; F:glyoxylate reductase (NADP) activity; IDA:EcoCyc.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IDA:EcoCyc.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   HAMAP; MF_01666; 2_Hacid_dh_C_GhrA; 1.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR023514; GhrA.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; NAD; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    312       Glyoxylate/hydroxypyruvate reductase A.
FT                                /FTId=PRO_0000076028.
FT   ACT_SITE    227    227       {ECO:0000250}.
FT   ACT_SITE    275    275       Proton donor. {ECO:0000250}.
SQ   SEQUENCE   312 AA;  35343 MW;  5B2F966D11DC6B40 CRC64;
     MDIIFYHPTF DTQWWIEALR KAIPQARVRA WKSGDNDSAD YALVWHPPVE MLAGRDLKAV
     FALGAGVDSI LSKLQAHPEM LNPSVPLFRL EDTGMGEQMQ EYAVSQVLHW FRRFDDYRIQ
     QNSSHWQPLP EYHREDFTIG ILGAGVLGSK VAQSLQTWRF PLRCWSRTRK SWPGVQSFAG
     REELSAFLSQ CRVLINLLPN TPETVGIINQ QLLEKLPDGA YLLNLARGVH VVEDDLLAAL
     DSGKVKGAML DVFNREPLPP ESPLWQHPRV TITPHVAAIT RPAEAVEYIS RTIAQLEKGE
     RVCGQVDRAR GY
//
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