ID   Q7S550_NEUCR            Unreviewed;      1134 AA.
AC   Q7S550;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=Fatty acid oxygenase {ECO:0000313|EMBL:EAA30613.1};
GN   ORFNames=NCU05858 {ECO:0000313|EMBL:EAA30613.1};
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA30613.1, ECO:0000313|Proteomes:UP000001805};
RN   [1] {ECO:0000313|EMBL:EAA30613.1, ECO:0000313|Proteomes:UP000001805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC   {ECO:0000313|Proteomes:UP000001805};
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA   FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA   Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA   Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA   Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA   Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA   Lander E.S., Nusbaum C., Birren B.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002242; EAA30613.1; -; Genomic_DNA.
DR   RefSeq; XP_959849.1; XM_954756.2.
DR   AlphaFoldDB; Q7S550; -.
DR   STRING; 367110.Q7S550; -.
DR   PeroxiBase; 5308; NcLDS01.
DR   PaxDb; 5141-EFNCRP00000005686; -.
DR   EnsemblFungi; EAA30613; EAA30613; NCU05858.
DR   GeneID; 3876022; -.
DR   KEGG; ncr:NCU05858; -.
DR   VEuPathDB; FungiDB:NCU05858; -.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   InParanoid; Q7S550; -.
DR   OMA; RHYTIDY; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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; 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; 2.
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   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001805};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         431
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ   SEQUENCE   1134 AA;  126012 MW;  1B262FB33313AA63 CRC64;
     MSSHQNGTNG HSASTSDNGK ESKSRNVIGP DPKAERTASM AKPRPTSMKL PFTGASRQGV
     ENAFERHRQT IQSAVQPLPT QQGAGTFSEN KKWGKLSSDL MTLRWADIKT LKHMVVAKIK
     GERLADDKTM IMEKVIQLVS NLPSNSKLRV ELTNGFLGEL WYTLEHPPSI YVGEYYQYRK
     ADGSCNNIMF PQLGAAGTTY ARSVRPNVIR QGALPDPELI FDSVMKRTEY KSHPNNVSSI
     LWYWASIIIH DLFWTDYRDM SKSKTSSYLD LSPLYGSNQD MQDTIRTFKD GKLKVDCYAD
     KRLLGMPPGV SVLLIFFNRF HNYTCDNLIA INEDGRFNKP SPKLEGEKAE AAWKKYDNDL
     FQTARLITSG LYINITLLDY VRNIVNLNRV DTTWTLDPRA DTGIDVGTKD GAERGTGNVV
     SAEFNLCYRW HSCISAKDEA WIEDFYYELF GKPGSDLSFH ELIMGFGKFE GGIPADPADR
     PIRKDKGHFS RDANGKISDD ELAECIADAI EDPAGSFGAK NVPPSMRAVE ILGIIQGRKW
     NLAGLNEFRK HFGLKPYETF EDINSDPGVS EALRRLYDHP DFVELYPGIV AEEHKSPMVP
     GVGIAPTYTI SRVVLSDAVC LVRGDRHYTI DYNPRNLTNW GYNEVQYDLN LKHGCVFYKL
     FMRALPNHFK ENSVYAHYPM VTPAENKKIL TDLKRDHLFD WARPTRQPKP HQVKTHAGAQ
     HVLDNDKEGT SGAYMSSWHA GLESLLGKPL SNNNPDAHDS QRRDIHEQLY SAEWADQVKA
     FFAQTTDALL AGESYNVGGH LLVDLVRDVG NIVPTLFAAK VFGISLQTKN NTNGLYTPQE
     LYAVLAVIFA AIFYDHDPVK THQLRDAART VATQLGTALE SAVKSQTSFF GSLLGGGGSG
     SNNNALTAYG NDLVKRLSKA GLSASDVAFG QVLPIVASSV PSIAEAFASA ADFYLGEKGQ
     AHLGAIQELA RQPASASADA QLLGYVLEGI RLSGNALGAF RQASAVDAIK EEDGSEVRVQ
     PGDRVFVSVK SAAQSPTTFP SPEEVNPSRP LEAYKIFFFG THSYLGHEVS QIALREMFRS
     LFKRSNVRRA PGPQGQLKKI TRELNEELSQ TFYLREDWGA VTPFPVTMKV TWDE
//