DKGA_ECOLI
ID DKGA_ECOLI Reviewed; 275 AA.
AC Q46857; Q2M9I7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=2,5-diketo-D-gluconic acid reductase A;
DE Short=2,5-DKG reductase A;
DE Short=2,5-DKGR A;
DE Short=25DKGR-A;
DE EC=1.1.1.274;
DE AltName: Full=AKR5C;
GN Name=dkgA; Synonyms=yqhE; OrderedLocusNames=b3012, JW5499;
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=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 [2]
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 [3]
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).
RN [4]
RP CHARACTERIZATION.
RX PubMed=11934293; DOI=10.1021/bp0101841;
RA Habrych M., Rodriguez S., Stewart J.D.;
RT "Purification and identification of an Escherichia coli beta-keto ester
RT reductase as 2,5-diketo-D-gluconate reductase YqhE.";
RL Biotechnol. Prog. 18:257-261(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 2-275.
RX PubMed=16284956; DOI=10.1002/prot.20710;
RA Jeudy S., Monchois V., Maza C., Claverie J.-M., Abergel C.;
RT "Crystal structure of Escherichia coli DkgA, a broad-specificity aldo-keto
RT reductase.";
RL Proteins 62:302-307(2006).
CC -!- FUNCTION: Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG)
CC to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective
CC -keto ester reductions on ethyl acetoacetate and other 2-substituted
CC derivatives.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-D-gluconate + NADP(+) = 2,5-didehydro-D-gluconate +
CC H(+) + NADPH; Xref=Rhea:RHEA:23828, ChEBI:CHEBI:11449,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16808, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.274;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5.;
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; U28377; AAA69179.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76048.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77069.1; -; Genomic_DNA.
DR PIR; B65088; B65088.
DR RefSeq; NP_417485.4; NC_000913.3.
DR RefSeq; WP_000013149.1; NZ_SSZK01000023.1.
DR PDB; 1MZR; X-ray; 2.13 A; A/B=2-275.
DR PDBsum; 1MZR; -.
DR AlphaFoldDB; Q46857; -.
DR SMR; Q46857; -.
DR BioGRID; 4262381; 26.
DR STRING; 511145.b3012; -.
DR jPOST; Q46857; -.
DR PaxDb; Q46857; -.
DR PRIDE; Q46857; -.
DR DNASU; 947495; -.
DR EnsemblBacteria; AAC76048; AAC76048; b3012.
DR EnsemblBacteria; BAE77069; BAE77069; BAE77069.
DR GeneID; 66673093; -.
DR GeneID; 947495; -.
DR KEGG; ecj:JW5499; -.
DR KEGG; eco:b3012; -.
DR PATRIC; fig|1411691.4.peg.3717; -.
DR EchoBASE; EB2835; -.
DR eggNOG; COG0656; Bacteria.
DR HOGENOM; CLU_023205_0_1_6; -.
DR InParanoid; Q46857; -.
DR OMA; AFKPGNE; -.
DR PhylomeDB; Q46857; -.
DR BioCyc; EcoCyc:MON0-148; -.
DR BioCyc; MetaCyc:MON0-148; -.
DR BRENDA; 1.1.1.346; 2026.
DR SABIO-RK; Q46857; -.
DR EvolutionaryTrace; Q46857; -.
DR PRO; PR:Q46857; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0050580; F:2,5-didehydrogluconate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:EcoCyc.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; 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 CDD; cd19131; AKR_AKR5C2; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044504; AKR5C2.
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.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ascorbate biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..275
FT /note="2,5-diketo-D-gluconic acid reductase A"
FT /id="PRO_0000124599"
FT ACT_SITE 51
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187..241
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1MZR"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:1MZR"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1MZR"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1MZR"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1MZR"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:1MZR"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:1MZR"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:1MZR"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1MZR"
FT TURN 188..192
FT /evidence="ECO:0007829|PDB:1MZR"
FT TURN 194..198
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:1MZR"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:1MZR"
FT TURN 270..274
FT /evidence="ECO:0007829|PDB:1MZR"
SQ SEQUENCE 275 AA; 31110 MW; 0FF6E140411BAD43 CRC64;
MANPTVIKLQ DGNVMPQLGL GVWQASNEEV ITAIQKALEV GYRSIDTAAA YKNEEGVGKA
LKNASVNREE LFITTKLWND DHKRPREALL DSLKKLQLDY IDLYLMHWPV PAIDHYVEAW
KGMIELQKEG LIKSIGVCNF QIHHLQRLID ETGVTPVINQ IELHPLMQQR QLHAWNATHK
IQTESWSPLA QGGKGVFDQK VIRDLADKYG KTPAQIVIRW HLDSGLVVIP KSVTPSRIAE
NFDVWDFRLD KDELGEIAKL DQGKRLGPDP DQFGG
