ID   B0CTV0_LACBS            Unreviewed;      1062 AA.
AC   B0CTV0;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Linoleate diol synthase {ECO:0000313|EMBL:EDR13977.1};
GN   ORFNames=LACBIDRAFT_305274 {ECO:0000313|EMBL:EDR13977.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR13977.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR   EMBL; DS547092; EDR13977.1; -; Genomic_DNA.
DR   RefSeq; XP_001874536.1; XM_001874501.1.
DR   AlphaFoldDB; B0CTV0; -.
DR   GeneID; 6071081; -.
DR   KEGG; lbc:LACBIDRAFT_305274; -.
DR   HOGENOM; CLU_002329_0_0_1; -.
DR   InParanoid; B0CTV0; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000001194; 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: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:UP000001194}.
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         381
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   1062 AA;  118218 MW;  5B448757A184D49D CRC64;
     MSVNRLSSFL GRRPSASTTG VANGTATETS PTNGASGDPK ILKDFREQIK RGVPFSLETS
     SLAAILDLIR HKDAIDDRKL LLEHALTFVS RLEEGDLSRK LKNGIIELLY NDLTHPAATS
     ISNKYAWRTA DGSYNNIDVP DMGKAGTPYS RSVQQSNPLP KNQLPDPGLV FDTLLKREGF
     VKHPGGLSSL MFSFAALVIH SVFRTSHRDI NINETSSYVD LAPLYGNNVE DQNRIRVRDG
     RGRLHPDVFA EDRLLLLPPQ VCVLLVLFSR NHNYIVERLL EINERGTYVD PDQLSPDDPA
     QKAQLLAQEE ELFQTGRLIN CGWFGSVVFS DYFSCILGLV RDGNNWSLSP FGEIRKDDHS
     LFERGKGNVC SVEFNCLYRW HATTSLEDEA WVHKAFSQIF GGKPIDQITP EDFRNAAKRL
     EQVQPDVTHW TFGGLQRQEN GRFKDSDLAD VLKNATEHSA GAFRARGTPA AMRLNEVMGI
     EQNRRWGVCS LNDFRKYLGL KPYATFLEWN SDPEIADSAE KLYGDINFLE LYVGLQAEEA
     KPLVEGAGLC PGYTISRAIL SDAIALTRGD RYFTHDFTPF NLTAWGFADC QRDPNAFGFG
     STLGRLFLRT LPNDYTENSV YTFFPLMTPE SMKTNLTKLN LLDKYDLSRP QTRTPLKIVS
     DHTEVVKLLK DKESTSKPYA ARVARVIKGK GFFPAEGGKE QEAVTTALSG SPELVDDIGK
     YFYETTKKLI VDNSFTLVGG KVAGVDLVKH VLRVVPVLWV ATDLAGIELK TKSHPHGPYT
     PSELFDVLGE IYAFVFLDVE LAKVMVLQES IKSHVKKLLR LIKGGLDGGA GNRLSIAGIV
     ETVSSLFSKP KKSDHSVLMK RLHELGQSHD QLANTVLALM VGASVELSLS LTNMVNLYLG
     SDKQAQITAL AKNPDSSLKG YVYEALRIDP PFEGVYRIST KDQTIAGQTV NKNDRIFVDI
     GTANLNEKVF PHPVAVDISR STKEALFAEG VFEYLGEHLT VKVMGEVLRA VFDLNNVSRA
     PGQSGVLKRF KVHTRPECRY GYLNHSQIAY EWPTSMAIQY SK
//