ID A2QJ58_ASPNC Unreviewed; 1080 AA.
AC A2QJ58;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN ORFNames=An04g05880 {ECO:0000313|EMBL:CAK38852.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK38852.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK38852.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; AM270079; CAK38852.1; -; Genomic_DNA.
DR RefSeq; XP_001401954.1; XM_001401917.1.
DR AlphaFoldDB; A2QJ58; -.
DR PeroxiBase; 5298; AnLDS01.
DR EnsemblFungi; CAK38852; CAK38852; An04g05880.
DR GeneID; 4990997; -.
DR KEGG; ang:ANI_1_966184; -.
DR VEuPathDB; FungiDB:An04g05880; -.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000006706; Chromosome 6L.
DR GO; GO:0051213; F:dioxygenase activity; ISA:AspGD.
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: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; PROSTAGLANDIN G/H SYNTHASE; 1.
DR PANTHER; PTHR11903:SF37; PSI-PRODUCING OXYGENASE A; 1.
DR Pfam; PF03098; An_peroxidase; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
SQ SEQUENCE 1080 AA; 120354 MW; 92B611103B567B36 CRC64;
MSGANNHSIV NGIGSTISQV EKAISASLRP LPTATGNGTY ITEPDQTGIV KDLSHVDFTD
IKALLEVIKD AVTGQPVDDR HYIMERVIQL AAGLPSTSKN GKDLTNAFLK QLWNDLEHPP
ISYLGRDSSY RKADGSGNNF LWPHIGAAGS HYARSVRPTT VQSPSLPDPS TLFASLLERK
EYKEHPNKIS SVLFYLASVI IHDLFQTDRS DFTLNKTSSY LDLSPLYGNN QDEQDLVRTF
KDGKLKPDCF SSKRVLGFPP GVGVLLLMFN RFHNYVVENL ATINEGGRFT KPDESDVDAS
TKYDNDLFQT GRLVTCGLYI NIILKDYVRT ILNINRTDSL WSLDPRADIQ DSLLGSAPAE
ATGNQVSAEF NLVYRWHACI SQRDEKWTQD LYKDLFPGKD PNNVSLQEFI RGVAKWEASL
PEQPPDRPFA GLQRNADGAF DDGDLANMFA DGVEDCAGAF GAGNIPSVFR NIEALGILQA
RSWNLATLNE FRKFFDLAPY KTFEEINPDP YIAAQLKNLY DEPDLVEMYP GVIVEATKDA
IVPGSGLCTN FTISRAILSD AVSLVRGDRF YTVDYTPKHL TNWAYNEIQP QDSVDQGQVF
YKLVLRAFPN HFKGDSVYAH FPLVIPSENK KILEKLSVAQ DYSWGRPSYT PLPQFISSNA
ACISVLNDQE AFKVTWGSKI 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 RDMSLYAHFG FGPHQCLGMG ICKLALTTML
RVVGRLDNLR RAPGSQGQLK KIAGPGGISM YMTADQSSYW PFPSTMKIQW DGDLPSLATN
//