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Database: UniProt
Entry: F9G4L7_FUSOF
LinkDB: F9G4L7_FUSOF
Original site: F9G4L7_FUSOF 
ID   F9G4L7_FUSOF            Unreviewed;       544 AA.
AC   F9G4L7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=FOXB_13599 {ECO:0000313|EMBL:EGU75896.1};
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:EGU75896.1};
RN   [1] {ECO:0000313|EMBL:EGU75896.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU75896.1};
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 zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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:EGU75896.1}.
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DR   EMBL; AFQF01003390; EGU75896.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9G4L7; -.
DR   STRING; 660025.F9G4L7; -.
DR   PaxDb; 5507-FOXG_10144P0; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   CDD; cd08249; enoyl_reductase_like; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR047122; Trans-enoyl_RdTase-like.
DR   PANTHER; PTHR45348; HYPOTHETICAL OXIDOREDUCTASE (EUROFUNG); 1.
DR   PANTHER; PTHR45348:SF2; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C2E1P3.01; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..544
FT                   /note="Enoyl reductase (ER) domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003390289"
FT   DOMAIN          216..542
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   544 AA;  58544 MW;  C373F4D2E8F7E9D4 CRC64;
     MISLRDIGLL LLAAPIAMAA PKAPSEVTIK TLPFSKPEDT SKAPSTSAVA SPASDAAQKA
     ACQLPLRFTN FALYSDTGCK NVIFDPFMLT WDPCKGYQWT NALANGVIFQ SMRWTGGNAD
     GDKKVLLADQ QYDKLFRAVL SYSYIFDVYY YTKPSLEQLR LYIAYSSNHF TGLAYSILVL
     LALSAFHLIS SYLCNPYSMS HTFEPNVAAV LPVKEGQLTI QQRPVPTPKE GELLVRNAVV
     AANPSDWKIQ ALGLSTNFPA VLGSDLSGIV ISIGPGVTRF KPGDRVIGFA LGVISENIEK
     AAFQTYTLLD EVATTHLPDN ISFEEGSVLP VGMLTAAIAL FDGLGLPMRE RIVDEDGAIL
     VWSGASAVGV SAVQIAHALG WTVYATASPK HDEWLKTLGA AEAWDYRDPQ VTQKIAEALK
     ASGTKIRGVI DARAEGSSFD SVAEILNAAD LTPGCKVTAL MPWPEETSLP AGIEGHHTNC
     VGFTVNYPDI ATWVFGGWLS KALKDGRIKP APRVRVIEGG LEATQETLNL LRAGASGEKF
     VLKV
//
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