ID B8MWJ7_ASPFN Unreviewed; 317 AA.
AC B8MWJ7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Cytochrome P450, putative {ECO:0000313|EMBL:EED56760.1};
GN ORFNames=AFLA_074540 {ECO:0000313|EMBL:EED56760.1};
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 {ECO:0000313|EMBL:EED56760.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED56760.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
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).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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; EQ963472; EED56760.1; -; Genomic_DNA.
DR RefSeq; XP_002372372.1; XM_002372331.1.
DR AlphaFoldDB; B8MWJ7; -.
DR EnsemblFungi; EED56760; EED56760; AFLA_074540.
DR VEuPathDB; FungiDB:AFLA_003003; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_877096_0_0_1; -.
DR OMA; KCIEQTE; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.10.630.10; Cytochrome P450; 2.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF215; CYTOCHROME P450 MONOOXYGENASE CICH-RELATED; 1.
DR Pfam; PF00067; p450; 2.
DR SUPFAM; SSF48264; Cytochrome P450; 2.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 317 AA; 36831 MW; D1EC53895F40CEE7 CRC64;
MIGTVLDTVL GNPQGAVGGL FVGSFVIFWV VPFLYNLFFS PLRNVPGPFW ARFTILWEFS
QLMKGRSHEE YIKLHKKYGP VVRVSPKRYS VIDPQDVKKI YGFGADFPKS EFYDSLGDPK
NIFTVRDNED HKDRRRKVAS LYTMSSMVAY EDAVDRMTTL CIKKMTDLAA SRKLISIPKF
MQFYAFDVIG EITFDQNFGM MENMGDTQGI IKEIHAMNNT IVYGPDADQY RPERWLEDKP
QPDYRDSMMF AFGSGSRTCI GRNISLLEIT KVLPQIVRKF DLKFEEKKDP WDAWCAWFVY
PKYKCWIEPR KPVENVA
//
