ID A0A0J9WRZ6_FUSO4 Unreviewed; 1101 AA.
AC A0A0J9WRZ6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Prostaglandin-endoperoxide synthase 1 {ECO:0000313|EMBL:KNB13397.1};
GN ORFNames=FOXG_12909 {ECO:0000313|EMBL:KNB13397.1};
OS Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS / NRRL 34936) (Fusarium vascular wilt of tomato).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=426428 {ECO:0000313|EMBL:KNB13397.1, ECO:0000313|Proteomes:UP000009097};
RN [1] {ECO:0000313|EMBL:KNB13397.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4287 {ECO:0000313|EMBL:KNB13397.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KNB13397.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4287 {ECO:0000313|EMBL:KNB13397.1};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; DS231712; KNB13397.1; -; Genomic_DNA.
DR RefSeq; XP_018251442.1; XM_018392847.1.
DR AlphaFoldDB; A0A0J9WRZ6; -.
DR GeneID; 28954207; -.
DR KEGG; fox:FOXG_12909; -.
DR VEuPathDB; FungiDB:FOXG_12909; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000009097; 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; 2.
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 Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000009097}.
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 408
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 1101 AA; 123784 MW; BB15760978A25E94 CRC64;
MAEHKNGVAT NGYEKKSSPA SSSTKSEAKP LPNSDKKDGI VKSFKQLRVA SKRPLPKEMG
DGSYRVVENR PGLKQDIRRL RGRDLKTLLE IVKAKVKGET QQDDKTMIME RTIQLVANLS
DHSKVQESLT NSFISQLWNS IDHPPMLYMG DKFRFRQPDG SNNNPYLPQL GAARTPYSRT
VRPKGMSLGA QPDPEAIFES VFARDAFRKN PNNVSSILWY WATIIIHDLF WTNLQDPNQN
DSSSYLDLAP LYGSTEKDRD SIRTFKDGQL KPDCFADKRL IGNPPGVPIL LIMFNRFHNH
VATNLADINE GGRFSKPAEH LSPEAADAAW KKRDTELFET ARLVTSGLYI NITLIDYVRN
IINLNRVDTT WTLDPRQEMG VSVGTKDLSE SGTGNVVSAE FNLCYRWHSC LSEMDDKWVQ
DFYTELLGEN YGPMNLQTMM KALKAFEASV ADEPSERTFG GFKRGPDGKF NDDELVEALA
TAIEQPGGAF GGRNVPRIMK PIEMLGIMRG RKWNLAGLNE FRKHFGLKAY ETFEDINSDP
SVADALRNLY QHPDYVELYP GIVAEEAKTP MVPGVGIAPT YTISRVVLSD AVALVRGDRY
YTTDYNPRHL TNWGYKEVDY DLKVNHGCVF YKLFLRAFPQ HFKGNSVYAH YPMVIPSENE
KILTNIKRAD RFDFSRPEPT ATRINIIGYN AAKYILEDQQ KYRVCWEEGL KHLMGEAGGR
FMLSGDTALH AQQRKCMGKL LYNDTWRNAV KSFYATTAEK LLAEKSYRLA GKMQVDVVRD
VGNVAHTHFV ARMFNLPLKT SENPKGVFSE QELYMILAVI FVCIFFDIDP AKSFPLRQGA
REVAQKLGGI IEMNVKLANS IGVKGLFTSK PDKNDDPLAR YGENMAKGLK KAGLSTEDIV
WSQILPTAGA MVPNQAQVFA QTLDWYLSPA GEKYRPELAR IAALETGDET DALLLGYAME
GIRMAGTFGL YREATGPDTI HEDDGRSIPV NAGDRVFVSF VQAAQDPKIF PNPGVVDPKR
PLDKYIHYGV GPHACLGRDI SQVALTELFR AVFRKKGVRR VPGAQGELKK VPRPGGFFVY
MTEDWGSIWP FPTSMKITWD E
//
