ID B7MA75_ECO45 Unreviewed; 275 AA.
AC B7MA75;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=2,5-diketo-D-gluconate reductase A {ECO:0000313|EMBL:CAR04624.1};
DE EC=1.1.1.274 {ECO:0000313|EMBL:CAR04624.1};
GN Name=dkgA {ECO:0000313|EMBL:CAR04624.1};
GN OrderedLocusNames=ECS88_3392 {ECO:0000313|EMBL:CAR04624.1};
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR04624.1, ECO:0000313|Proteomes:UP000000747};
RN [1] {ECO:0000313|Proteomes:UP000000747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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DR EMBL; CU928161; CAR04624.1; -; Genomic_DNA.
DR RefSeq; WP_000013152.1; NC_011742.1.
DR AlphaFoldDB; B7MA75; -.
DR KEGG; ecz:ECS88_3392; -.
DR HOGENOM; CLU_023205_0_1_6; -.
DR Proteomes; UP000000747; Chromosome.
DR GO; GO:0050580; F:2,5-didehydrogluconate reductase activity; IEA:UniProtKB-EC.
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; NADP-dependent oxidoreductase domain; 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; 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE; 1.
DR PANTHER; PTHR43827:SF3; ALDO-KETO REDUCTASE; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 2.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 4: Predicted;
KW Ascorbate biosynthesis {ECO:0000256|ARBA:ARBA00022644};
KW Oxidoreductase {ECO:0000313|EMBL:CAR04624.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000747}.
FT DOMAIN 18..261
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 51
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 76
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 275 AA; 31138 MW; 0FF6E1405FFB4353 CRC64;
MANPTVIKLQ DGNVMPQLGL GVWQASNEEV ITAIQKALEV GYRSIDTAAA YKNEEGVGKA
LKNASVNREE LFITTKLWND DHKRPREALL DSLKKLQLDY IDLYLMHWPV PAIDHYVEAW
KGMIELQKEG LIKSIGVCNF QIHHLQRLID ETGVTPVINQ IELHPLMQQR QLHAWNATHK
IQTESWSPLA QGGKGVFDQK VIRDLADKYG KTPAQIVIRW HLDSGLVVIP KSVTPSRIVE
NFDVWDFRLD KDELGEIAKL DQGKRLGPDP DQFGG
//
