GHRA_ECOLI
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 03-AUG-2022, entry version 153.
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., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT 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 ycdW
RT 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 hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and
CC hydroxypyruvate into glycolate and glycerate, respectively. Inactive
CC towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate and pyruvate.
CC Only D- and L-glycerate are involved in the oxidative activity with
CC 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; EC=1.1.1.79;
CC 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; EC=1.1.1.81;
CC Evidence={ECO:0000269|PubMed:11237876};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH;
CC Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57783, 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 25
CC 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. {ECO:0000269|PubMed:11237876}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. GhrA subfamily. {ECO:0000305}.
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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_SSZK01000090.1.
DR PDB; 6OVL; X-ray; 2.10 A; A=1-312.
DR PDB; 6OXN; X-ray; 2.61 A; A=1-312.
DR PDB; 6P35; X-ray; 2.50 A; A=1-312.
DR PDBsum; 6OVL; -.
DR PDBsum; 6OXN; -.
DR PDBsum; 6P35; -.
DR AlphaFoldDB; P75913; -.
DR SMR; P75913; -.
DR BioGRID; 4260060; 17.
DR BioGRID; 850788; 1.
DR IntAct; P75913; 1.
DR STRING; 511145.b1033; -.
DR jPOST; P75913; -.
DR PaxDb; P75913; -.
DR PRIDE; P75913; -.
DR EnsemblBacteria; AAC74117; AAC74117; b1033.
DR EnsemblBacteria; BAA35814; BAA35814; BAA35814.
DR GeneID; 66670699; -.
DR GeneID; 946431; -.
DR KEGG; ecj:JW5146; -.
DR KEGG; eco:b1033; -.
DR PATRIC; fig|1411691.4.peg.1238; -.
DR EchoBASE; EB3628; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_6; -.
DR InParanoid; P75913; -.
DR OMA; VQMAEYV; -.
DR PhylomeDB; P75913; -.
DR BioCyc; EcoCyc:G6539-MON; -.
DR BioCyc; MetaCyc:G6539-MON; -.
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:0008465; F:glycerate dehydrogenase activity; IEA:RHEA.
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_Enterobacterales.
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 3D-structure; Cytoplasm; Direct protein sequencing; NAD; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..312
FT /note="Glyoxylate/hydroxypyruvate reductase A"
FT /id="PRO_0000076028"
FT ACT_SITE 227
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6OXN"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6OXN"
FT HELIX 95..111
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:6OVL"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6OVL"
FT TURN 202..206
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6OVL"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:6OVL"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6OVL"
FT HELIX 282..297
FT /evidence="ECO:0007829|PDB:6OVL"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:6OVL"
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
