ID D3GT90_ECO44 Unreviewed; 294 AA.
AC D3GT90;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Aldo/keto reductase {ECO:0000313|EMBL:CBG33169.1};
GN OrderedLocusNames=EC042_0335 {ECO:0000313|EMBL:CBG33169.1};
OS Escherichia coli O44:H18 (strain 042 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=216592 {ECO:0000313|EMBL:CBG33169.1, ECO:0000313|Proteomes:UP000001407};
RN [1] {ECO:0000313|EMBL:CBG33169.1, ECO:0000313|Proteomes:UP000001407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=042 / EAEC {ECO:0000313|Proteomes:UP000001407};
RX PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT "Complete genome sequence and comparative metabolic profiling of the
RT prototypical enteroaggregative Escherichia coli strain 042.";
RL PLoS ONE 5:E8801-E8801(2010).
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DR EMBL; FN554766; CBG33169.1; -; Genomic_DNA.
DR AlphaFoldDB; D3GT90; -.
DR KEGG; elo:EC042_0335; -.
DR PATRIC; fig|216592.3.peg.356; -.
DR HOGENOM; CLU_023205_0_1_6; -.
DR Proteomes; UP000001407; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd19133; AKR_AKR5F1; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 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; 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; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 4: Predicted;
KW Ascorbate biosynthesis {ECO:0000256|ARBA:ARBA00022644}.
FT DOMAIN 28..267
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 54
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 83
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 294 AA; 33200 MW; EB91F18D4554C068 CRC64;
MEGLTVEFSV LSNNLKMPMM GFGVFQVTDK DVCKQSVLNA IRTGYRLIDT AAVYGNEDAV
GEAVREAISE GLCTREELFI TSKLWVQDML NQDIAAAGIE ASLKKSGLEY FDLFLLHQAM
RDYFSAWRAL EDAYEEGKLK AIGVSNFYPH VLANFCETVR VKPMVNQVEL HPYFAQPEAL
ATMKYYNVQP EAWAPLGGGR HKPFENNLLQ SIADAHQKSI SQVILRWNIQ RGVVVIPKST
HQQRIEENFA IWDFSLTEKE MAQISSLDLG YVGESVKHFN PEFVRGCLAV KIHD
//
