DKGA_YERPE
ID DKGA_YERPE Reviewed; 277 AA.
AC Q8ZI40; Q0WIZ6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=1.1.1.346;
DE AltName: Full=AKR5C;
GN Name=dkgA; Synonyms=ara14; OrderedLocusNames=YPO0676, y3501, YP_2991;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG)
CC to 2-keto-L-gulonic acid (2KLG). {ECO:0000250}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
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; AL590842; CAL19352.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM87049.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS63169.1; -; Genomic_DNA.
DR PIR; AF0083; AF0083.
DR RefSeq; WP_002212175.1; NZ_WUCM01000053.1.
DR RefSeq; YP_002345742.1; NC_003143.1.
DR AlphaFoldDB; Q8ZI40; -.
DR SMR; Q8ZI40; -.
DR STRING; 214092.YPO0676; -.
DR PaxDb; Q8ZI40; -.
DR DNASU; 1148448; -.
DR EnsemblBacteria; AAM87049; AAM87049; y3501.
DR EnsemblBacteria; AAS63169; AAS63169; YP_2991.
DR GeneID; 57973951; -.
DR KEGG; ype:YPO0676; -.
DR KEGG; ypk:y3501; -.
DR KEGG; ypm:YP_2991; -.
DR PATRIC; fig|214092.21.peg.937; -.
DR eggNOG; COG0656; Bacteria.
DR HOGENOM; CLU_023205_0_1_6; -.
DR OMA; AFKPGNE; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0051596; P:methylglyoxal catabolic process; IBA:GO_Central.
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; 2.
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 3: Inferred from homology;
KW Ascorbate biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..277
FT /note="2,5-diketo-D-gluconic acid reductase A"
FT /id="PRO_0000124603"
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"
SQ SEQUENCE 277 AA; 31520 MW; ED9C2945F0EBD140 CRC64;
MTMQPLIKLY DGRLMPQLGL GVWQASIQET ELAVSKALEV GYRSIDTAAI YKNEEGVGKA
LKAAAVARDE LFITTKLWND DQHNPQQALE TSLQKLQLDY VDLYLIHWPD PKQDHYVSAW
RELVTLKEQG LIRSIGVCNF HIPHLQRLID ETGIAPTVNQ IELHPLLQQR QLHAWNATHH
IATESWSPLA QGGKGVFDQE IIRKLAQQYN KTPAQIVIRW HLDSGLIVIP KSVTPARIRE
NFEVFDFKLQ KEELLAITKL DCGKRLGPDP EVFGSDR
