ID X0CVY2_FUSOX Unreviewed; 716 AA.
AC X0CVY2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=FOQG_04031 {ECO:0000313|EMBL:EXK95463.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK95463.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK95463.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK95463.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH658366; EXK95463.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CVY2; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_014528_0_0_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.400.10; Acetoacetate decarboxylase-like; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR010451; Acetoacetate_decarboxylase.
DR InterPro; IPR023375; ADC_dom_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF261; SALICYLATE HYDROXYLASE_MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13860)-RELATED; 1.
DR Pfam; PF06314; ADC; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF160104; Acetoacetate decarboxylase-like; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663}.
FT DOMAIN 11..369
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 587..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 78331 MW; 0EAD10C63A6848BC CRC64;
MTQDTETRPL DILIVGAGIG GLTAALGLRQ QGHKVTLFER SQLAKEVGAA IHLAPNCHGI
LKRFGVFPES FGANRVEGVT EYTGDGHLKF DNNLKGPLSV WEHPWVLAHR VSLHENLKNQ
ATSHEGPGTP AILKTSSPVV DVDPSTATVK FEDGTTVSGD LVLGADGVSS ITRSIVTGSD
IKPYGSGKSA FRFMIPHSDI LKNEKARPFA ERTGTMTMWM GDDRRLVMYP CSNNTVMNFV
AIHPSSITSG ANKGSGWGNG GSKELLREVY KDFEPRVLAL LDLVDVSELK LWTLLDMDRI
STWHKDRLVL LGDAAHPFLP HQGQGGGIAI EDAASLVALF PPGTTANDVP SRLALYEKIR
DERAHTVQSF TRQAGEDLNE EKRAQFNIFK FLNYNFGHDE WHNTKKALRD YLWSQNKNLH
WKSPVSFGPM PSPRQDFHGQ RYNGNGSSFT TWSVRFKSSA PYLKTLFPTD RFSFYKPGTV
AEATYSCTEL KDMKWLGGGG YKFFGLWIHG VQYEKKDGSK IYGSFLAVLL ENLADPIVTG
REELGMPKLF CDIDVVEKGA NTSIRCSWRG AEFVDITLKG LGEATNGHTN GVNGTNGVNG
TNGHHPPVGP PGAPPLPEEQ GLLLYRYVPA VGQPGVADAA YPVFIEDGLE TTKRQVEKTL
VGSGGDLDLT AGTWDTLPTL NHIATGFSQI PVYGVVKSKV EYGRGVDDIS HARRVD
//