ID A0A0S7E0H5_9EURO Unreviewed; 1079 AA.
AC A0A0S7E0H5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN ORFNames=ALT_008542 {ECO:0000313|EMBL:GIM40055.1}, CNMCM8060_001899
GN {ECO:0000313|EMBL:KAF4180151.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM40055.1};
RN [1] {ECO:0000313|EMBL:GIM40055.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM40055.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4180151.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4180151.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF4180151.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4180151.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) 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:GIM40055.1}.
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DR EMBL; BCLY01000009; GIM40055.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000014; KAF4180151.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7E0H5; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_5662; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000713487; 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; 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 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}.
FT BINDING 377
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 1079 AA; 121130 MW; 03758CB3237D17E9 CRC64;
MSEKQTGSAN GGLAKTLAQL EQVVSASLRP LPSQTGDGTY VTEQVKTGIL KDLPHVDLGD
LKTLVDVSKS ALTGEALDDR KYIMERVVQL AAGLPSTSQI GKELTNTFLT TLWNDLEHPP
ISYLGRDAMY RRADGSGNNV LWPHIGAAGT PYARSVRPKT TQSPNLPDPE TLFDCLLARK
EYKEHPNKIS SVLFYIASII IHDLFQTDRK DPAISLTSSY LDLSPLYGNN QEEQNLVRTF
KDGKLKPDCF STKRILGFPP GVGVVLMMFN RFHNYVVEKL AMINEGGRFT KPQESDTAAY
AKYDNDLFQT GRLVTCGLYV NIILKDYVRT ILNINRTNSI WSLDPRSEMK DGLLGSAAAQ
ATGNQVAAEF NLVYRWHSCI SQRDQKWTED MYQELFPGQD PSNISLQDFL RGLGRWEAKL
PEEPQERPFA GLQRKADGSY DDDDLVKIFE ESVEDCAGAF GALHVPTVFR SIEALGIQQA
RSWNLATLNE FRKYFNLAPY KTFEEINPDP HVADQLKRLY DHPDRVEIYP GIILEDAKES
MAPGSGLCTN FTISRAILSD AVALVRGDRF HTVDFTPKHL TNWAYSEIQP QDSVDQTHVF
YKLVLRAFPN HFRGDSIYAH FPLVVPSENK KILSKLGTAD KYSWDRPNYT PPPQFINSHS
ACMSILSDQE TFKVTWGSKI EFLMRHNNQP YGRDFMLSGD RTPNAMSRQM MGKALYRDKW
ETEVKKFYED ITLKLLHRYS YKLAGVNQVD IVRDIANLAQ VHFCASVFSL PLKTESNPRG
IFTESELYQI MAVVFTSIFY DADVGKSFEL NQGARGVTQQ LGQLTLANVE LIEKTGFIAN
LVHSLHRHDV LSEYGVHMIQ RLLDSGMPAP EIVWTHVLPT AGGMVANQAQ LFSQSLDYYL
SEEGSVHLPE INRLAKEDTP EADDLLLRYF MEGARMRSSV ALPRVVAQPT VVEDNGQKIT
LKQGQHIICN LVSASMDPVS FPEPDKVKLD RDMNLYAHFG FGPHQCLGLG LCKTALTTML
KVIGRLDNLR RAPGGQGHLK KLSGPGGIAM YMTADQAGFF PFPTTMKIQW DGDLPELKE
//
