ID I1S2G6_GIBZE Unreviewed; 1097 AA.
AC I1S2G6; A0A098E179;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Linoleate 10R-lipoxygenase {ECO:0008006|Google:ProtNLM};
GN Name=FG10960.1 {ECO:0000313|EnsemblFungi:CEF87352};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EnsemblFungi:CEF87352};
RN [1] {ECO:0000313|EnsemblFungi:CEF87352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF87352};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF87352}
RP GENOME REANNOTATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF87352};
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).
RN [3] {ECO:0000313|EnsemblFungi:CEF87352}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF87352};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; HG970334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011325412.1; XM_011327110.1.
DR AlphaFoldDB; I1S2G6; -.
DR EnsemblFungi; CEF87352; CEF87352; FGRRES_10960.
DR GeneID; 23557836; -.
DR KEGG; fgr:FGSG_10960; -.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OrthoDB; 3322316at2759; -.
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 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}.
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 404
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 1097 AA; 123069 MW; 961597E620AD7136 CRC64;
MASNQVKNGA VASNGYGKEK SPSSASSSQK NEVPAPPHNK SEGLVKSIKK LRLASKRPLP
TEMGDGSYRQ VATRPGLKQD VRRLRGKDLK TLLEIISSKL KGEMQQDDKT MIMERTIQLV
ANLSDHSKVQ EALTNSFIAQ LWNSIDHPPM LYMGNKYRFR QPDGSWNNPY LPQLGAARTP
YSRTVRPKGM SLGAQPDPEA IFESVFARGI FRKNPNNVSS ILWYWATIII HDPDQNDSSS
YLDLAPLYGS TVKDRDSIRT FKDGQLKPDC FADKRLIGNP PGVPIILIMF NRFHNHVATN
LADINEGGRF SKPGAHLDAE AAAAAWKKRD EELFETARLV TSGLYINITL IDYVRNIINL
NRVDTTWTLD PRQEMGVSVG TKNLSESGTG NVVSAEFNLC YRWHSCLSEM DEKWVEDFYT
ELLGENYGPM NLQTMMRALK AFEATVAEEP SERTFGGFKR GPDGKFNDDE LVEALATAIE
QPGGAFGGRN VPRIMKPIEM LGIMRGRKWN LAGLNEFRKH FGLKAYDTFE DINSDPEVAD
ALRNLYQHPD YVELYPGIVA EEAKTPMVPG VGIAPTYTIS RVVLSDAVAL VRGDRYYTID
YHPRNLTNWG YKEVDYDLNI NHGCVFYKLF LRAFPQHFKG NSVYAHYPMV IPTENHKILT
DLKRVDRFDF SRPAPTATRI NIVGYKAAKY ILEDQAKYRV CWEEGLKHLM GEGGGRFMLS
GDTALHAQQR KCMGRLLYND TWRNAVKSFY STTAEMLLNE KSYTLAGKKQ VDVVRDVGNV
AHTHFVARMF NLPLKTKQNP KGVFSEQELY MILAVIFVCI FFDIDPAKSF PLRQAAREVA
QQLGKIVEMN VKLATSVGIK GLFTSKPNKN DDPLAAYGEN MAKGLKKAGL SIDDIVWSQI
LPTAGAMVPN QAQVFAQTLD WYLSPAGEKY RPELHRIAAL ETGDETDALL LGYAMEGIRM
AGTFGLYREA TTADVIQEDD GREVPVKAGD RVFVSFVTAA KDPNIFPDPE VVDPRRPLDS
YIHYGVGPHA CLGRDISQVA LTELFRALFR KKGLRRVAGA QGELKKVPRP GGFFVYMTED
WGSIWPFPTS MKVTWDE
//
