ID   B8NWN9_ASPFN            Unreviewed;      1138 AA.
AC   B8NWN9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Fatty acid oxygenase, putative {ECO:0000313|EMBL:EED45847.1};
GN   ORFNames=AFLA_120760 {ECO:0000313|EMBL:EED45847.1};
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:EED45847.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED45847.1, 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   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR   EMBL; EQ963485; EED45847.1; -; Genomic_DNA.
DR   RefSeq; XP_002384783.1; XM_002384742.1.
DR   AlphaFoldDB; B8NWN9; -.
DR   STRING; 332952.B8NWN9; -.
DR   EnsemblFungi; EED45847; EED45847; AFLA_120760.
DR   VEuPathDB; FungiDB:AFLA_014077; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   OMA; NTEYART; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; 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:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd20612; CYP_LDS-like_C; 1.
DR   CDD; cd09817; linoleate_diol_synthase_like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR034812; Ppo-like_N.
DR   PANTHER; PTHR11903:SF13; LINOLEATE 10R-LIPOXYGENASE; 1.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1138 AA;  128540 MW;  862A397DF2F0B00B CRC64;
     MKGVPSSAEA SNSSPGSSLP SQRAHEPLTH KQPTLDHPRK QSVQSISSEH GGMAENFSKI
     TKVVQAARRP LPTETGDGTY IEPENGGSLW RDLRALGIKD ANTLKDLIEN KAGGLVKGSG
     QVVDDKTMLM ERIIQLVAKL PTESRNRVKL TNMFLGELWD SLPHPPLSYV GDKYAYRSAD
     GSYNNPTLPW LGAANTEYAR TIEPLKVRPA SLPDPGLVFD SLFARDTFNP HPNNVSSVFF
     TWASLIIHDI FQTGHPDENF NKTSSYLDLS ILYGDNQEEQ NMMRTFKDGK IKPDSFSEPR
     LHALPAACGV ILVMLNRFHN HVVEQLAAIN ENGRFTKPPE RILDPVEARA AWAKYDNDLF
     QTGRLITCGL YINITLYDYL RTIVNLNRDN TTWTLDPRAH MEHDTVPTAL GNQCSVEFNL
     AYRWHSTISR KDEAWTEQAY QAIVGKPGSE ATVEDLMSGM RRLGANMPKD PSKREFAGLK
     RQSSGKFKDE ELVDILTMAI DEVAGSFGAR NVPKVLRSVE ILGMEQARRW NVGSLNEFRK
     FFDLKPYQSF EEINSDPEVA DQLRHLYEHP DNVELYPGIV AEEAKKPMIP GVGIAPGYTV
     SRAVLSDAVA LVRGDRFYTE YNSRNLTNWG YEEANYDLEI NQGCVFYKLA LRAFPQYFKQ
     NSIFAHYPMT TPSANRDIMK MLGREEDFSW DRPSYTPPRT TLFDYANVRR ILEDSSNFRV
     IWDEATGYVF GKGGYDFMLS GDSPFHANQR RIMKESLYRS QWHEAVKEFY LEITEQLLSE
     KSCRVGNVNQ IDISRDVGNL AHVHFASNIF SLPLKTKEHP HGVLTEHEMF DVMSIIFTAI
     FFDVDPSKSF RLRHMARKAA ETLGPLVEAN VKAVSSASFL STLIDGIRTN KNALSGYGVH
     MIRRLLDHGL DASEVTWSQI LPTAVAMVPN QAQVFTQIID YYLSDEGKEH LLNIQQLAKE
     DTPASDEMLL RYVMEAIRLN GIFGSYRKSH TNLTLDDKNK MVQIKPGDTV FVSFVDANRD
     PNVFPNPKKV DLNRPMESYI HYGVGPHTCL GGEASKVALT AMLRVVGRLK NLRRAPGPQG
     ELKKIPRDHG FYTYMRADET SLYAFPMTWK LHYDGTIPGR ERSVPEKLTC NVPGHWHD
//