ID F9XCR4_ZYMTI Unreviewed; 939 AA.
AC F9XCR4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Linoleate diol synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MYCGRDRAFT_100421 {ECO:0000313|EMBL:EGP86918.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP86918.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP86918.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; CM001201; EGP86918.1; -; Genomic_DNA.
DR RefSeq; XP_003851942.1; XM_003851894.1.
DR AlphaFoldDB; F9XCR4; -.
DR EnsemblFungi; Mycgr3T100421; Mycgr3P100421; Mycgr3G100421.
DR GeneID; 13393719; -.
DR KEGG; ztr:MYCGRDRAFT_100421; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_0_0_1; -.
DR InParanoid; F9XCR4; -.
DR OMA; EEPAHAF; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000008062; Chromosome 6.
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 Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 2.
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 PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 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; 2.
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:UP000008062}.
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265
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 939 AA; 102840 MW; C9B5C310EA70536C CRC64;
MAVGQLKSLL GSIRRKPSTA PDRRSREETN GVNGEKTSLM SDLSSIGVKN VKMLGGALVD
MAGGEPLDDK QLLLENGVSM LQSLPSNSGL GSTVSNGFIG MLWNDLPHPA ATLAGPESRY
RRHDGGGNNP WQPEMGKAGT PYSRSVPPVK PKGPNLPDVE LVFEQLLKRD GAFREHPSGL
NRLFFSFATI SLQDNDIFQL SRNINVGFFA TVVLKDYVAA ILNTPRANSE WSLDLGAEIK
KGGSRVERGT GNVVSTEFAV LYHWHAALSA ADAQWMEDII RESAPEIGHI DDVTAETFTK
VVKTQGHKLM STEPRLWTFG GIKRGADGRF SDNDLGEILK NCVDEPAHAF GAHGTPASLK
VVDLMGQLQA RNHFKVCTMN EFRTYLNLKA YESFEDWNPD KKTARAAELL YGHIDNLELY
PGLMAECTKP AMPGSGVCPG QTTGRGILDD AVALVRGDRF LSYDFNSNTL TNWGFAKLGS
LPGGSYGGML PHLLFTGLPG AYKGTSPYAL LPFYTPKAVA GILKGNKAID RYDLNRNRSD
GGIVAVHSQA GCKQVFEDEQ TFRPAFSMDK TNFLPKVFFT DGFDGKITKY FSETVARLIK
DSSLKYAGSK RSVDIVRDVT NVAPIMWLAE HFAIPLKTAR TPKGLLSLPQ LFDMYMVTFL
YQNFNILPIN EWKLRDGYQK AEPVLRNIFE THLKTQQGFK ETIVDRLAKG SAYEVGPEAD
RLYHALNDSK LPTRDLVTDC IGMGAPVAGI VTQQASLLIA FYLRPDNSQH KGRIVQLAHQ
NDAASESQLQ GYVLEGMRHA GVVPGLPRVA TKDVVVEDGA NGSVRIKRDQ TVLIATSSSS
KDASAFADPD TIDPSRPRES YFMLRSGLHA DFGSKLVLPA LAATLREVFK LKNVRAAPGK
NGMFTTTRHV VAGVVLTHYL DDNARESPFP TSLTVEYDE
//
