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Database: UniProt
Entry: F9F2J9_FUSOF
LinkDB: F9F2J9_FUSOF
Original site: F9F2J9_FUSOF 
ID   F9F2J9_FUSOF            Unreviewed;       435 AA.
AC   F9F2J9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=FOXB_00623 {ECO:0000313|EMBL:EGU88879.1};
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:EGU88879.1};
RN   [1] {ECO:0000313|EMBL:EGU88879.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU88879.1};
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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:EGU88879.1}.
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DR   EMBL; AFQF01000176; EGU88879.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9F2J9; -.
DR   STRING; 660025.F9F2J9; -.
DR   PaxDb; 5507-FOXG_15312P0; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR46720; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR   PANTHER; PTHR46720:SF3; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..380
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   435 AA;  48174 MW;  B2D33B61758B3FE0 CRC64;
     MAKPSRNEIH VAIIGAGIGG LALAMALHKK DISFTLYEDA KEYSAVGAGI GFAPNGMRTM
     DLIEPGFRPF YEAICVGNKG EKAQDIFFEG MLLEEGLGRD KPWYGHSGWG HPDYIRKSAH
     RKTLLDIMTS FIPIENVKFN KRLTNIEQRP DGVTLSFLDG TTAECSVLAG ADGIKSTVRA
     NVLEQYPSQI APVYAGAYCY RAVIPMSEAY EILGDLTDVA KFYFGPKRSA VTYRITGGDE
     FNYLLCVADS PDGWKLKGAV TEAISHEAMM ADFEGPGVDD RFRQLLAKAK PVKWGFFHHF
     RTASYYRDRV ALVGDSAHAS LPFQAAGAAQ GLEDALVLSN VLAEVAKIPE RGAELAPFIQ
     AGLSAYDSVR RPRAQKQLEQ AAEVGRMIFF QHEEAGDDMD KILPRLQQGR FNWLWFHDMN
     DDAQEAVKRM QKEIS
//
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