ID   FLUA_ASPFN              Reviewed;         510 AA.
AC   B8NYW9;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Cytochrome P450 monooxygenase AFLA_114810 {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=AFLA_114810;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2]
RP   IDENTIFICATION OF THE GENE CLUSTER 41.
RX   PubMed=20447271; DOI=10.1111/j.1364-3703.2009.00594.x;
RA   Georgianna D.R., Fedorova N.D., Burroughs J.L., Dolezal A.L., Bok J.W.,
RA   Horowitz-Brown S., Woloshuk C.P., Yu J., Keller N.P., Payne G.A.;
RT   "Beyond aflatoxin: four distinct expression patterns and functional roles
RT   associated with Aspergillus flavus secondary metabolism gene clusters.";
RL   Mol. Plant Pathol. 11:213-226(2010).
RN   [3]
RP   FUNCTION.
RX   PubMed=27647242; DOI=10.1016/j.funbio.2016.07.010;
RA   Chang P.K., Scharfenstein L.L., Ehrlich K.C., Diana Di Mavungu J.;
RT   "The Aspergillus flavus fluP-associated metabolite promotes sclerotial
RT   production.";
RL   Fungal Biol. 120:1258-1268(2016).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster 41
CC       that mediates the biosynthesis of an extracellular and diffusible
CC       metabolite that is able to stimulate colony sclerotial production
CC       (PubMed:27647242). {ECO:0000269|PubMed:27647242}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:27647242}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; EQ963487; EED44779.1; -; Genomic_DNA.
DR   RefSeq; XP_002385534.1; XM_002385493.1.
DR   AlphaFoldDB; B8NYW9; -.
DR   SMR; B8NYW9; -.
DR   EnsemblFungi; EED44779; EED44779; AFLA_114810.
DR   VEuPathDB; FungiDB:AFLA_114810; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_14_0_1; -.
DR   OMA; MPYTRKG; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..510
FT                   /note="Cytochrome P450 monooxygenase AFLA_114810"
FT                   /id="PRO_0000438559"
FT   BINDING         444
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
SQ   SEQUENCE   510 AA;  58796 MW;  FA47C2547AA36D06 CRC64;
     MLILLGLLCL YTGLYVARTY WRLRHFPGPL VARFTDLGRL WWVKTSRSHH HHMGLHSRYG
     QYVRLGPNMI SISDPDAIPL VYPIRPGVPK SDFYRSMMPY TRKGRSLPLV FNTRDEDLHK
     RLKTPIAHLY SLSNILTFEA FVDQVLEILF RQFEERFVPD QAPFNLGNWL QYFAFDVMGT
     MSFSRRYGFL EKGRDDTGLL SAIWAFMKAA APVTQMPWVD LVWNKNPFIA LFRATPAQPI
     LNVVLSRIND RRNELYSTTS TPEKVNERDF LSRFMHIQSN SDTIPPWAVT AWSFSNVIAG
     SDTTAVAMKT LWYNLLLHPA TMHRLRKELV QAQQQSKLSH PFPAWNEISG LPYLNACVNE
     ALRIHPPFCL PFERIVPAEG MTIGDHFFPG GTVIGMNPWV INRHRPTFGE DADAWRPERW
     LEDPARTRQM ENTLLSFGAG RRVCLGKNIA LLELKKLTSA LVLHYELEIV NPEKFQSQNF
     FFFKQEGLYA AVKRRSAGSP ELYPDDAVPH