DKGB_ECOLI
ID DKGB_ECOLI Reviewed; 267 AA.
AC P30863; P77777;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=2,5-diketo-D-gluconic acid reductase B;
DE Short=2,5-DKG reductase B;
DE Short=2,5-DKGR B;
DE Short=25DKGR-B;
DE EC=1.1.1.346;
DE AltName: Full=AKR5D;
GN Name=dkgB; Synonyms=yafB; OrderedLocusNames=b0207, JW0197;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nishimura K., Komine Y., Miyamoto K., Kitabatake M., Mathunaga F.,
RA Hisano T., Miki T., Inokuchi H.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 194-195.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=6255418; DOI=10.1093/nar/8.17.3809;
RA Sekiya T., Mori M., Takahashi N., Nishimura S.;
RT "Sequence of the distal tRNA1Asp gene and the transcription termination
RT signal in the Escherichia coli ribosomal RNA operon rrnF(or G).";
RL Nucleic Acids Res. 8:3809-3827(1980).
RN [7]
RP CHARACTERIZATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=10427017; DOI=10.1128/aem.65.8.3341-3346.1999;
RA Yum D.-Y., Lee B.-Y., Pan J.-G.;
RT "Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-
RT gluconate reductases in Escherichia coli.";
RL Appl. Environ. Microbiol. 65:3341-3346(1999).
CC -!- FUNCTION: Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG)
CC to 2-keto-L-gulonic acid (2KLG).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-L-idonate + NADP(+) = 2,5-didehydro-D-gluconate +
CC H(+) + NADPH; Xref=Rhea:RHEA:35111, ChEBI:CHEBI:11449,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36602, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.346;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0.;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: 2-keto-L-gulonic acid is a key intermediate in the
CC production of L-ascorbic acid (vitamin C).
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; D12650; BAA02170.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08629.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73312.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77878.2; -; Genomic_DNA.
DR EMBL; V00336; CAA23619.1; -; Genomic_DNA.
DR PIR; A64745; A64745.
DR RefSeq; NP_414743.1; NC_000913.3.
DR RefSeq; WP_000997010.1; NZ_STEB01000020.1.
DR AlphaFoldDB; P30863; -.
DR SMR; P30863; -.
DR BioGRID; 4261784; 5.
DR IntAct; P30863; 1.
DR STRING; 511145.b0207; -.
DR jPOST; P30863; -.
DR PaxDb; P30863; -.
DR PRIDE; P30863; -.
DR EnsemblBacteria; AAC73312; AAC73312; b0207.
DR EnsemblBacteria; BAA77878; BAA77878; BAA77878.
DR GeneID; 66671503; -.
DR GeneID; 944901; -.
DR KEGG; ecj:JW0197; -.
DR KEGG; eco:b0207; -.
DR PATRIC; fig|1411691.4.peg.2077; -.
DR EchoBASE; EB1601; -.
DR eggNOG; COG0656; Bacteria.
DR HOGENOM; CLU_023205_0_1_6; -.
DR InParanoid; P30863; -.
DR OMA; WRHPDEP; -.
DR PhylomeDB; P30863; -.
DR BioCyc; EcoCyc:MON0-149; -.
DR BioCyc; MetaCyc:MON0-149; -.
DR BRENDA; 1.1.1.274; 2026.
DR SABIO-RK; P30863; -.
DR PRO; PR:P30863; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:EcoCyc.
DR GO; GO:0047681; F:aryl-alcohol dehydrogenase (NADP+) activity; IDA:EcoCyc.
DR GO; GO:1990002; F:methylglyoxal reductase (NADPH-dependent, acetol producing); IDA:EcoCyc.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0051596; P:methylglyoxal catabolic process; IMP:EcoCyc.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43827; PTHR43827; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW Ascorbate biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..267
FT /note="2,5-diketo-D-gluconic acid reductase B"
FT /id="PRO_0000124604"
FT ACT_SITE 39
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179..231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 194..195
FT /note="RI -> AY (in Ref. 1; BAA02170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 29437 MW; 265C7B1CC2D9C2E5 CRC64;
MAIPAFGLGT FRLKDDVVIS SVITALELGY RAIDTAQIYD NEAAVGQAIA ESGVPRHELY
ITTKIWIENL SKDKLIPSLK ESLQKLRTDY VDLTLIHWPS PNDEVSVEEF MQALLEAKKQ
GLTREIGISN FTIPLMEKAI AAVGAENIAT NQIELSPYLQ NRKVVAWAKQ HGIHITSYMT
LAYGKALKDE VIARIAAKHN ATPAQVILAW AMGEGYSVIP SSTKRKNLES NLKAQNLQLD
AEDKKAIAAL DCNDRLVSPE GLAPEWD
