ID   A0A2J6TA91_9HELO        Unreviewed;      1069 AA.
AC   A0A2J6TA91;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Linoleate diol synthase {ECO:0000313|EMBL:PMD59940.1};
GN   ORFNames=K444DRAFT_561624 {ECO:0000313|EMBL:PMD59940.1};
OS   Hyaloscypha bicolor E.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX   NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD59940.1, ECO:0000313|Proteomes:UP000235371};
RN   [1] {ECO:0000313|EMBL:PMD59940.1, ECO:0000313|Proteomes:UP000235371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E {ECO:0000313|EMBL:PMD59940.1,
RC   ECO:0000313|Proteomes:UP000235371};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR   EMBL; KZ613803; PMD59940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6TA91; -.
DR   STRING; 1095630.A0A2J6TA91; -.
DR   InParanoid; A0A2J6TA91; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000235371; 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; 3.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235371}.
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         372
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   1069 AA;  118683 MW;  03B0D87195147E02 CRC64;
     MGSNPFRALF GTIKKKPAKA PDGQTDAEAA PGGKPGDENP VKTSILHDLT HLDLKEAETM
     AQALTTIVSQ KPMNDKELLL ENGVSMLQSL PLNSGLSQTI SNDFIAMLYR DLPHPPPTRA
     GHPARYREND GSGNNPWTPG MGKAGSPYSR SVPPSKPKGP NLPDPELVYD QLLKRTGPFR
     EHPSGLNRLF FSFATIVIHE CFQTSRSDPW INETSSYVDL STLYGNTGKE QKRVRTHHNG
     LIFPDSIASE RIMMMPPGVV AVLLMFSRNH NSIAKNLLVI NESGKYGAWE KLTDKEKTWQ
     DEDIFQLARN INVGFFASVV LHDYVAAILN TPRANSTWSL DLGAEIKQLG VRVDRGRGNV
     VSVEFAVLYH WHAALSAADD KWMQYVLKDA EPGLKSMDDV DLDVYKRVMY KGGHDLLAKK
     AKEWTFGGLK RGPDGRFSDY DLAEIIKGCI EEPAHAFGAH GTPQSLKIVD ILGQLQARES
     FNVCTMNEFR RYLNLQEYKS FEEWNPDKET ARAAELLYGH IDNLELYPGL MAECTKPAMP
     GSGVCPGQTT GRGILDDAVA LVRGDRFLSY DFNSSTLTNW GFAKLCSITP GAYGGVLPHL
     LFNGLPAAWT GTSPYVLLPF YTPKAANGIL EQNKVINLYD LERPKSDMEI IGIHTHEGCK
     KVFEDRENFV VMYQKAIRDC TNGHDFMIGW DDPARHDPRS SLLHKVFFEA GFEENVTTFF
     RSNVSRLISE HSLKYSNSTR RSIDIVRDVT NVVPILWLAQ RFAIPLKARE TPHGLISIPD
     LFMSYLVLFM YQSFNILPAS EWTLRDGARK AAIGLREIFD AHLKTASGIT SEIVDWLAEG
     TAFEVSAQAK RLYEELLKSK LPIGDLVGDC IGMGAPVAGN ITQQASLLID LYLSAGYEEY
     KDRIIELSKL DTPEAERELQ GFVFEGMRHA GAVPGLPRIA TKDITVEDGA HGPVSIKKGH
     TVLIATSVAA MDPKQFPNPE KLDPHRPFED YILLGHGLHY CFGARLIGSS LAATLREVFK
     LKNVQRGKGG GGSFMRVEEE FAGVRFTKYL DANAAESPIP TTLTIEYEE
//