ID   C9SDY1_VERA1            Unreviewed;      1070 AA.
AC   C9SDY1;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Linoleate diol synthase {ECO:0000313|EMBL:EEY17228.1};
GN   ORFNames=VDBG_03337 {ECO:0000313|EMBL:EEY17228.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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DR   EMBL; DS985216; EEY17228.1; -; Genomic_DNA.
DR   RefSeq; XP_003007198.1; XM_003007152.1.
DR   AlphaFoldDB; C9SDY1; -.
DR   STRING; 526221.C9SDY1; -.
DR   GeneID; 9533768; -.
DR   KEGG; val:VDBG_03337; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   OMA; RHYTIDY; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000008698; 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; 2.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1039..1070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1064
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         421
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   1070 AA;  119486 MW;  30513A8B61F9432D CRC64;
     MKKDSNASHA SSGSSTQPGR IDPAVNGNVR NAERKAKPIG DDVCGGHDEK SGKLAQFMKL
     RKASKRPLPK DHGDGSYVIV PARPGVVQNL KVLRKRDIQT LATMIKGKLK GEKIKDDKTM
     IMEYVIQMVA KLPHNSSLRE KLTNTLIEEL WDSLDHPPLL FVGDDWKYRR ADGSHNNPLY
     PWLGAAGQTY ARSVAPKKPT LAALPDPGLI FDSIFARNEY TKHPNNVSSI LWNWATIIIH
     DLFWTDFRDI NKSKTSSYLD LSPLYGSNQD MQDTIRTFKD GKLKADSFAD KRLLGMPPTV
     SVLLIMFNRF HNHVAENLAA INEGGRFTPP SPFLEGEAAE AASKKYDNDL FQTARLVTSG
     LYINITLVDY VRNIVNLNRT NTTWTLDPRQ ESGMQVDTAE GAESGTGNMV SAEFNLCYRW
     HSCISDKDDK WIQQFYGEIL GGHQGELSPA EMGRIFMQYE RSIPDDPIER TFGGYKRGEN
     GKFSDDDLVD CVSASVEDPA GSFGARNVPK VMRPVEILGM LQARKWNVAG LNEFRKHFGL
     KPYDRFEDIN SDPKVSEALR NLYQKPDNVE LYPGIVAEEA KSPMVPGVGI APTYTISRVV
     LSDAVCLVRG DRHYTTDYNP RYLTNWGFNE ANYDLKINHG CVFYKLFIRA FPNHFKHNSV
     YAHYPMVIPS ENHKILTDLG RVDLFNFDRP AFTPLRVNVT SYGGAQHVLE NKAAYRVTWH
     EGLGAQMDEG GHKFMLAGDT DFHAGQKQCM ASQLYKTDWH AAVRKFYADI TEQLLQEKSY
     TLGNTRRRHV DLVRDVGNIT HVHFASRVFN LPLKTAANPK GVFSEQELYQ LLAVIFVGIF
     FDLDPVKSFP LRQAAREASQ TLGKVIETNV KLATTLGIRG LFTGKADKND PLAAYGTNLV
     KGLKLSGLNN YDIAWSQILP TAGAMCPTKH KFFVGAARDA AHFPEPGGRG PRRPLGAYIH
     YGLGPHACLG REASQVALTE MFRGLFRRRN VRREPGPQGE LKKVPRPGGF FVYLREDWGG
     VWPFPCSMKV MWDEDEVANG ATNGTTNGAT NGATNGQEGS AYESKDKATA
//