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Database: UniProt
Entry: E5C3T7_9BACE
LinkDB: E5C3T7_9BACE
Original site: E5C3T7_9BACE 
ID   E5C3T7_9BACE            Unreviewed;       283 AA.
AC   E5C3T7;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=NADP-dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF00248};
GN   ORFNames=BSGG_0823 {ECO:0000313|EMBL:EFS30123.1};
OS   Bacteroides sp. D2.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=556259 {ECO:0000313|EMBL:EFS30123.1, ECO:0000313|Proteomes:UP000003135};
RN   [1] {ECO:0000313|EMBL:EFS30123.1, ECO:0000313|Proteomes:UP000003135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D2 {ECO:0000313|EMBL:EFS30123.1,
RC   ECO:0000313|Proteomes:UP000003135};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Strauss J.,
RA   Sibley C., White A., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. D2.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFS30123.1}.
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DR   EMBL; ACGA02000065; EFS30123.1; -; Genomic_DNA.
DR   RefSeq; WP_009000866.1; NZ_JH636026.1.
DR   AlphaFoldDB; E5C3T7; -.
DR   HOGENOM; CLU_023205_0_1_10; -.
DR   OrthoDB; 9804790at2; -.
DR   Proteomes; UP000003135; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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;
FT   DOMAIN          21..257
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   ACT_SITE        48
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT   SITE            73
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ   SEQUENCE   283 AA;  32260 MW;  16C62EDFE85E88E8 CRC64;
     MEKVKLNNGI EMPILGYGVY QVTPEECERC VSDAISVGYR SIDTAQAYHN EEGVGNAISK
     CGVPRGELFI TTKVWISNAG YEKAKASIDE SLRKLKSDYI DLLLIHQPFG DYYGTYRAME
     EAYKAGKLRA IGVSNFYPDR FIDLAEFCEI TPAINQVETH VFNQQIKLQE VMKEYGTKIM
     SWGPFAEGRN DFFTNPTLQE IGKEYSKSVA QVALRYLIQR DIIVIPKSTH KERMIENFNV
     FDFSLTPDDM AAIAALDTAK TLFFSHYDPE MVKWLINYST KNE
//
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