ID A0A428QFB0_9HYPO Unreviewed; 1153 AA.
AC A0A428QFB0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN ORFNames=CEP53_004243 {ECO:0000313|EMBL:RSL63987.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL63987.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL63987.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL63987.1,
RC ECO:0000313|Proteomes:UP000287544};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSL63987.1}.
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DR EMBL; NKCJ01000068; RSL63987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428QFB0; -.
DR STRING; 1325737.A0A428QFB0; -.
DR Proteomes; UP000287544; 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:SF13; LINOLEATE 10R-LIPOXYGENASE; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
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:ARBA00022559};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000287544}.
FT BINDING 419
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 1153 AA; 128651 MW; 783FEA13463ACF0D CRC64;
MSSFNEKFQA GESYGDAKTG STALLDDPIK LATDIIKDYA GVRSQASIPE LAELIKELTV
EKGKPLDDKK GTTELLIGIL TSLPRTSKAR TQLTNKLIDT LWGNLQHPPL SYVGGDVKYE
VVNSNEPAHK HNCELYDTIE FKAPDSDVIL REQVPQAPDG LHQYRMPDGS FNNILEPNLG
RAGTPYAKSV RSEKRLHGVK PDPGLLFDLL LARDDKNFTE NPAGISSMLF YHAAIIIHDI
FRTSRTDPNK SDTSSYLDLA PLYGSSLKDQ LEIRTMKEGK LKPDTFHEKR LLGQPAGVNV
MLVLYSRFHN YVADILLKIN ENGRFTLQCP PNASAEDKAK AVAKQDHDLF NVARLITGGL
YINICLHDYL RAITNTHHSK SDWTLDPRVA IDKQFDGEGV PRGVGNQVSV EFNLLYRFHS
CISKKDEHWI NNFFLKLFPG RKAEDLQDVS WDELGQALIT FERNTPKDPS VRTFDGLERQ
ENGTFKDEDL VRILKEAMDD PAGTFGARMV PKALKVVEVL GIIQGRKWQV ASLNEFREFF
GLKKYDSFSE INSNPDIANI LEKLYTDPDM VELYPGLMIE DIKPARNPGS GIMPTYSVGR
AVLSDAVTLV RSDRFNTIDY TVSNLTAWGY NEVQQDYKTL GGSMLYKLIQ RGVPNWFPFN
SVAVMQPMYT KKANIAIAKE IGTYDQFSEA DPKPPAKPIV VTTNEAIKKT LSNPKQFVVP
WLQPLNTLFP GKKDYGWFML AGDEAKNFKH RADFQKAMAK VPNLHAAVHN MIERVGAKLI
EKETFKLKAG LEQIDIIRDV AIPLNTQLLA DLFYFDLRTD ENPDGTLGVA ELYRHLLNIR
IWGVNNNDPG QAWNRRRWAQ EGVTAVYNST KKLVDEAVLG RGMGLGIASA ISSKVGRKSY
LKKDSLRSCG LKLVEELLGQ GNNADQVTDN LWLTAFGGIG VPVTSFYEVL AFFLRPENAA
IWAEVQGIAQ KGDDATLHAY VAEAQRLTSS QRNVRIATAP AELEGKPVQP GTPVVMMLGM
AGRNGKEVPD ADKFNAQRKT DAVTAFSYGQ HECLAKDMAL AFVTGLIKLV ADLKRLRPAP
GQMGEVKTIQ VGTEKAYLND SWSYLGFDAS TWKVHFDGHG KGTFDGDRAP TATTPLQQYY
YMLQKRKDEI LGL
//
