GHRB_ECOLI
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 03-AUG-2022, entry version 177.
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 region
RT 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 TO
RP 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., 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 1-22, SUBUNIT, SUBSTRATE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9811658; DOI=10.1128/jb.180.22.5984-5988.1998;
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 chromosome,
RT 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 in the
RT 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 ycdW
RT and yiaE genes in Escherichia coli.";
RL Biochem. J. 354:707-715(2001).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and
CC hydroxypyruvate into glycolate and glycerate, respectively. Can also
CC reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D-gluconate (5KDG), 2-
CC keto-D-gluconate (2KDG) to D-gluconate, and 2-keto-L-gulonate (2KLG) to
CC L-idonate (IA), but it is not its physiological function. Inactive
CC towards 2-oxoglutarate, oxaloacetate, pyruvate, 5-keto-D-gluconate, D-
CC fructose and L-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; 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 -!- CATALYTIC ACTIVITY:
CC Reaction=D-gluconate + NADP(+) = 2-dehydro-D-gluconate + H(+) + NADPH;
CC Xref=Rhea:RHEA:16653, ChEBI:CHEBI:15378, ChEBI:CHEBI:16808,
CC ChEBI:CHEBI:18391, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.215; 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) {ECO:0000269|PubMed:11237876,
CC ECO:0000269|PubMed:9811658};
CC Vmax=345 umol/min/mg enzyme with glyoxylate as substrate (at pH 7)
CC {ECO:0000269|PubMed:11237876, ECO:0000269|PubMed:9811658};
CC Vmax=123 umol/min/mg enzyme with hydroxypyruvate as substrate (at pH
CC 7) {ECO:0000269|PubMed:11237876, ECO:0000269|PubMed:9811658};
CC Vmax=69 umol/min/mg enzyme with 2-oxo-D-gluconate as substrate (at pH
CC 7) {ECO:0000269|PubMed:11237876, 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 P37666; P36938: pgm; NbExp=2; IntAct=EBI-562547, EBI-542427;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed. {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=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB18530.1; Type=Frameshift; Evidence={ECO:0000305};
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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_SSZK01000068.1.
DR AlphaFoldDB; P37666; -.
DR SMR; P37666; -.
DR BioGRID; 4259301; 35.
DR DIP; DIP-10997N; -.
DR IntAct; P37666; 1.
DR STRING; 511145.b3553; -.
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 eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_6; -.
DR InParanoid; P37666; -.
DR OMA; KMKPNCI; -.
DR PhylomeDB; P37666; -.
DR BioCyc; EcoCyc:MON-43; -.
DR BioCyc; MetaCyc:MON-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: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; 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 Cytoplasm; Direct protein sequencing; Gluconate utilization; NAD; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..324
FT /note="Glyoxylate/hydroxypyruvate reductase B"
FT /id="PRO_0000076029"
FT ACT_SITE 237
FT /evidence="ECO:0000250"
FT ACT_SITE 266
FT /evidence="ECO:0000250"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="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
