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Database: UniProt
Entry: F9FMK0_FUSOF
LinkDB: F9FMK0_FUSOF
Original site: F9FMK0_FUSOF 
ID   F9FMK0_FUSOF            Unreviewed;       326 AA.
AC   F9FMK0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=NADP-dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF00248};
GN   ORFNames=FOXB_07630 {ECO:0000313|EMBL:EGU81835.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU81835.1};
RN   [1] {ECO:0000313|EMBL:EGU81835.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU81835.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC       {ECO:0000256|ARBA:ARBA00007905}.
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:EGU81835.1}.
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DR   EMBL; AFQF01002285; EGU81835.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FMK0; -.
DR   STRING; 660025.F9FMK0; -.
DR   PaxDb; 5507-FOXG_01819P0; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR   PANTHER; PTHR11732:SF218; NADPH-DEPENDENT ALDOSE REDUCTASE GRE3; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
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   3: Inferred from homology;
FT   DOMAIN          18..305
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   ACT_SITE        50
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT   SITE            79
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ   SEQUENCE   326 AA;  36709 MW;  C45028B78A22DE75 CRC64;
     MAPSTVKLAS GHEMPLVGFG LWKVPADQAA ETVYNAIKSG YRLFDGAYDY QNEKEAGQGI
     QRAIKEGLVK REDIFITTKL WNNYHAKEHA LAFAKSQNEA WGLGYIDLYL IHFPVALEYI
     EPEKRRYPAW WMDDQGTVKP ANVPIRETWE ALEEVVDQGI AKSIGVSNFQ AQSLYDVQRY
     TRHPISSLQI EHHPYLVQPD LIAMAQENNI AVTAYSSFGP QSFKELPGIF SKRAHGAEPL
     LESSLIKGIA GKYGKTPAQV LLRWATQRNV AVIPKSNNPS RLAQNLDVVS FDLSREEIES
     ISALDRGLRF NDPGFYLPNF PLRIFA
//
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