ID   A0A0D2D1U9_9EURO        Unreviewed;      1081 AA.
AC   A0A0D2D1U9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE            EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN   ORFNames=PV05_05052 {ECO:0000313|EMBL:KIW56387.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW56387.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW56387.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW56387.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-
CC         hydroperoxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25395,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:58659;
CC         EC=1.13.11.60; Evidence={ECO:0000256|ARBA:ARBA00000699};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR   EMBL; KN847319; KIW56387.1; -; Genomic_DNA.
DR   RefSeq; XP_013316971.1; XM_013461517.1.
DR   AlphaFoldDB; A0A0D2D1U9; -.
DR   STRING; 348802.A0A0D2D1U9; -.
DR   GeneID; 25326960; -.
DR   HOGENOM; CLU_002329_0_0_1; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000054342; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0052878; F:linoleate 8R-lipoxygenase activity; IEA:UniProtKB-EC.
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:UniProtKB-KW.
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; IPR017972; Cyt_P450_CS.
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; PS00086; CYTOCHROME_P450; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT   REGION          126..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         366
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   1081 AA;  119999 MW;  B806A9DE60FF86FD CRC64;
     MAAYVKQLLS LIWANPTHAP DGKTDAQAAA KTKVDQTSFL HDITRLKAKD LPTVLQGLTT
     IASGEPIDDK DLLLEHGISL LQSLPTNSGL SHSVGNSLIN LLWRDLPHPP GTLAGPDTKY
     RRHDGSGNSI WSPDMGKAGS PYSRSVPAMQ PKGPNLPDPE LVFEHLLKRK GPFRPHPSGL
     NRLFFSFATI VIHECFQTSR QNQWINETTS YLDLSTLYGN TEKEQKRVRT YNKGLIYLDS
     IASERIMLMP PGVIAVLLLF SRNHNHIAEN LLSINEAGKY GEWDTLSAEQ KKWQDEDIFQ
     IARNINVGFF VTVVLRDYVA AILNTPRANS EWSLDFNAEI KLAGSRVERG VGNVVSVEFA
     VLYHWHAALS AGDANWMEDL IRENLTELKS LDDMTPEMFW KVVKQEGHKL MSTEPRLWTF
     GGISRGGDGR FSDADLGKII KDCIEEPAHA FGAHGCPASM KVIEVMGMLQ AREVFNVCTL
     NEFRKYLNLK PYETFEDWAE DEDTARAAEL LYGHIDNLEL YPGLQAECTK PAMPGSGVSP
     SHTTGRGILD DAVALVRGDR FLTYDFNSST LTHWGVSKLS ETAPGAYGGM LPKMLFNALP
     GEFTGTSTYA LLPFYTPQAA KGILKGNKVI EKYDLKRPAS GVVTIVGIHT QEGLKTVTQD
     RDTFRTIYDS AIRTIANNHG FLLGWDEQKR HDERHAILHR AFFEDDFDAN ITRFFRERTR
     TLIANSSLHY ADSRRSIDIV RDVTNVVPVL WAAERFAIPL KTADHPRGLI SLAQLFDIYL
     VLFVSQTFNI LPQNEWKLRE AAQTVAPLLR SIFETHLRTQ AGGPQEAVVD WLAKGSAFEV
     GPDADRLYHA LRASDLPIGD LAADCIGLGT PIVGTITQQA SLLIDLYLSE GYETYKDRIV
     ELARQDRQDN TLSQDAAAAA AAAAAADREL LGFVYEGMRH AGFMPGLPRM AARDVTVQDG
     ARGPVHIKAH QIVLVANSKA AMDPVAFPDP QRLDPTRPLS AYTLFGHGMH KCFGERMTGK
     ALVAILREVF KLPNLRRANG RAGRFSIVEH EVAGVKLRAY LDGNSKESVV PTSLRLIYDD
     E
//