ID A0A3F3PP92_9EURO Unreviewed; 1080 AA.
AC A0A3F3PP92;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN ORFNames=BDQ94DRAFT_94411 {ECO:0000313|EMBL:RDH28747.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH28747.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH28747.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH28747.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) 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; KZ852073; RDH28747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3PP92; -.
DR STRING; 1341132.A0A3F3PP92; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000253729; 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; 1.
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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:RDH28747.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729}.
SQ SEQUENCE 1080 AA; 120368 MW; 027975B50C91CFB1 CRC64;
MSGANNHSIV NGIGSTISQV EKAISASLRP LPTATGNGTY ITEPDQTGIV KDLSHVDFTD
IKALLEVVKD AVTGQPVDDR HYIMERVIQL AAGLPSTSKN GKDLTNAFLK QLWNDLEHPP
ISYLGRDSSY RKADGSGNNF LWPHIGAAGS HYARSVRPTT VQSPSLPDPS TLFASLLERK
EYKEHPNKIS SVLFYLASVI IHDLFQTDRS DFTLNKTSSY LDLSPLYGNN QDEQDLVRTF
KDGKLKPDCF SSKRVLGFPP GVGVLLVMFN RFHNYVVENL ATINEGGRFT KPDESDVDAS
TKYDNDLFQT GRLVTCGLYI NIILKDYVRT ILNINRTDSL WSLDPRADIQ DSLLGSAPAE
ATGNQVSAEF NLVYRWHACI SQRDEKWTQD LYKDLFPGKD PNNVSLQEFI RGVAKWEASL
PELPPDRPFA GLQRNADGAF DDGDLANMFA DGVEDCAGAF GAGNIPSVFR NIEALGILQA
RSWNLATLNE FRKFFDLAPY KTFEEINPDP YIAAQLKNLY DEPDLVEMYP GVIVEATKDA
IVPGSGLCTN FTISRAILSD AVSLVRGDRF YTVDYTPKHL TNWAYNEIQP QDSVDQGQVF
YKLVLRAFPN HFKGDSVYAH FPLVIPSENK KILEKLSVAQ DYSWGRPSYT PLPQFISSNA
ACISVLNDQE TFKVTWGSKI EFLMRHNNHP YGRDFMLSGD KPPNAASRRM MGSALYRDKW
ESEVKRFYED ITIKLLRQHS YQLGGVNQVD IVRDVANYAQ VHFCANVFSL PLKTESNPRG
IFAESELYEI LALVFASIFY DADVGTSFQL NQTARDVTQQ LGELTMANVD FVNKAGFIAN
LVSSLHRHDV LSEYGEHMIQ RLLHSNVPPA EIVWTHLLPT AGGMVANQAQ LFSQCLDYYL
SDEGSIHLPD IKRLAKENTS EADALLLRYF MEGARLRSSV GLPRLVAKPT VVDDGGSKYT
LKPGQSVLCN LVSASMDPRS FPEPEKVKLD RDMNLYAHFG FGPHQCLGMG ICKLALTTML
RVVGRLDNLR RAPGSQGQLK KIAGPGGISM YMTADQSSYW PFPSTMKIQW DGDLPSLATN
//
