DKGA_ECO57
ID DKGA_ECO57 Reviewed; 275 AA.
AC Q8XBT6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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; OrderedLocusNames=Z4365, ECs3896;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG58148.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB37319.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58148.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB37319.1; ALT_INIT; Genomic_DNA.
DR PIR; H85960; H85960.
DR PIR; H91115; H91115.
DR RefSeq; NP_311923.2; NC_002695.1.
DR RefSeq; WP_000013136.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XBT6; -.
DR SMR; Q8XBT6; -.
DR STRING; 155864.EDL933_4234; -.
DR PRIDE; Q8XBT6; -.
DR EnsemblBacteria; AAG58148; AAG58148; Z4365.
DR EnsemblBacteria; BAB37319; BAB37319; ECs_3896.
DR GeneID; 916279; -.
DR KEGG; ece:Z4365; -.
DR KEGG; ecs:ECs_3896; -.
DR PATRIC; fig|386585.9.peg.4064; -.
DR eggNOG; COG0656; Bacteria.
DR HOGENOM; CLU_023205_0_1_6; -.
DR OMA; AFKPGNE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050580; F:2,5-didehydrogluconate reductase activity; IEA:InterPro.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW 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_0000124600"
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 275 AA; 31130 MW; A807C84DB1B7F78B CRC64;
MANPTVIKLQ DGNVMPQLGL GVWQASNEEV ITAIQKALEV GYRSFDTAAA YKNEEGVGKA
LKNASVNREE LFITTKLWND DHNRPREALL DSLKKLQLDY IDLYLMHWPV PAIDHYVEAW
KGMIELQKEG LIKSIGVCNF QIHHLQRLID ETGVTPVINQ IELHPLMQQR QLHAWNATHK
IQTESWSPLA QGGKGVFDQK VIRDLADKYG KTPAQIVIRW HLDSGLVVIP KSVTPSRIAE
NFDVWDFRLD KDELGEIAKL DQGKRLGPDP DQFGG
