ID Q7S550_NEUCR Unreviewed; 1134 AA.
AC Q7S550;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 119.
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).
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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: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
//