ID   F9WWV8_ZYMTI            Unreviewed;      1113 AA.
AC   F9WWV8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Linoleate diol synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MYCGRDRAFT_67035 {ECO:0000313|EMBL:EGP91582.1};
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:EGP91582.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP91582.1, 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; CM001196; EGP91582.1; -; Genomic_DNA.
DR   RefSeq; XP_003856606.1; XM_003856558.1.
DR   AlphaFoldDB; F9WWV8; -.
DR   EnsemblFungi; Mycgr3T67035; Mycgr3P67035; Mycgr3G67035.
DR   GeneID; 13398865; -.
DR   KEGG; ztr:MYCGRDRAFT_67035; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   InParanoid; F9WWV8; -.
DR   OMA; KIQWDGD; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000008062; Chromosome 1.
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:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 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:UP000008062}.
FT   REGION          20..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         378
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   1113 AA;  125227 MW;  70F5547F6E67B15F CRC64;
     MRKDTRKSME QLGTLLKAIR APLPTQTGDG SALPQPKKDT FSKDVREILR DIPRQDIDDI
     EGLIKVFKST AMGENLDDKE YLMESMIAVA TKLPESFLQD RLTTTLVTTL WNDLEHPPNV
     ILGEEYEFRQ PDGSNNNFKY PNVGKAGMPY ARTVNPKSKQ GGVLPDPGVL FDTVMARKHE
     AGEKHPNRIS SMLFYLASII IHDIFRTDHL DARISNTSSY LDLSPLYGSN WKEQKTMRTF
     QNGKIKPDCF AETRLLSFPP GCGALLIMFN RYHNYVVEQL ALINEDGRFT ENPRQVTVDR
     YGETGLNKRD DDLFQTARLI VCGLYINIIL IDYVRTILNL NRTDDNWQLD PRVDIPGGIP
     VATGNQCSAE FNLVYRWHSA VSERDDLWTQ QLFKELPLPD GLTAEDAAKP ENMKKFLMTL
     AHMQHDTESK DPTERDFPAL KSEKMDRIPE GPFKGNYKDD DLAALLTSSI EDCANAMGPQ
     QVPAVMKAIE ILGIQQARTW RCATLNEFRE HFHLKPHKTF EDITTNKEVS EALKHLYNTP
     DDVELYPGLV VEDDKQAKLP GSGLCPSYTT SRGVLSDAVA LVRGDRFYTT AYTPASLTNW
     GFQEASSDLS IDNGCVFYKL FLRALPNSYD PGSVYVHYPM TIPDEMKTIL QGLEKDHMYN
     FDKPKASHHP VTLFSHAAGM QVTENQEDFH VTWGPAMIFL MGPEAKNFML AGDGPENAKS
     RAMMEKTMYQ GIPSGNEKWL TAVRDFYEMK TTELLKQKSY KLAGVNNVDI IRDIGNLAHV
     HFCAELFSIP LKTEKFPLGI FTEQQLYLIM AAVFTCVFFD LDPPKSFPLR QKARAATQSL
     GNIMKAQVQS VKTFGKLAES LIDVVKPNDG PLGDYGVHMI AQLCKQDVDV DDLVWGNIMG
     TAGGMVANQG QLLGQALDYF FTTGKDHLPE INRLAKLDTP EADDTLMHYL MEGARLNGET
     AIFRTVTKDT TVVDNTPLLG EQVHHLKKGD TVFVNLKSAS RDAAAYPNPD ALDLTRDLNS
     YITLGHGVHQ CMGLPMTRVA LTTMLKVIGR LDNLRPAPVS VGTQSVGHSV KKVMKEFVPG
     DKHVLPEEWH YHLYLTEDWD QYFPFPTSKF EMV
//