ID A0A484F811_COLOR Unreviewed; 1126 AA.
AC A0A484F811;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN Name=LIDS {ECO:0000313|EMBL:TDZ13799.1};
GN ORFNames=Cob_v013117 {ECO:0000313|EMBL:TDZ13799.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ13799.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
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:TDZ13799.1}.
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DR EMBL; AMCV02000061; TDZ13799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A484F811; -.
DR STRING; 1213857.A0A484F811; -.
DR Proteomes; UP000014480; 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 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:UP000014480}.
FT REGION 136..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 384
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 1126 AA; 127042 MW; 90D7DD2C6B1E0431 CRC64;
MSQQLEEQFP KSSPALVERL AGVRKVVQKA ISPIPQHPEQ PPKSNSAQVE PSHLLQDVKH
LGFEDFDTLI NFFQSAVEGQ INDNELLLER LIQLFAKLPE NTDKGKKLEN GLIHQLWNGI
DHPPMTTLGD EHKYRSADGS ENSIHSPNMG KAGTPYARST PAKSYQNPDQ PEPDMIFDML
FARGSQFQPH PNKISSVLFY LATIITHDIF QTNGTSGINQ TSSYLDLSPL YGRNQTEQDE
MRTHRDGRLK PDTFSSKRVL GFPPGVGVML IMFNRFHNYT VAQLATINEN NRFPRPSEDV
PAESQRWKTY DNDLFQTARL ITTGLYASII LRDYVRTILN LNRSSSNWAL DPRTNEGKSI
LSQSTPEGTG NQVSVEFNLI YRWHNSISPR DEKWTKDVMK KVLGKDPSQM TLREFGAAMQ
KWEGEIPQDP AERGFMDLPR NADGTLREED LAKIFKESVE DVAGSYGANR IPEVMRPIEL
LGIVNSRKWN CATLNEFREH FGLTRHPTFE DINPEPDVAK KLRFLYGTPD AVELYPGLIA
EKAKPPMAPG SGLCGNFTMT RAILSDAVAL VRGDRFFTID YTPKNLTNWG YNESNYDKNV
DQSHVFYKLV YRAFPNSFQN NSIYAHFPFT VPSENKKILE SIDRAYLYTW DEPKTKSQLI
PIFSHKAVSD VLYNQQDFKV IWGEAINHLV AQPGKNYAKD FCLAGDGKAN LMNRTSVRKA
LIHGPWETEV WKWYSHTTPK LIEQNNFPIP NGRREIDVVR DVINLTNTRF NAALFCLPIK
NEDSPWGVYT DQELYMVLAT LFQCVFLDAD IANSFKLRTI ARELGQDLGK IVGLVAQTIS
KAGLITDIVA KIREGEASLP TFGNHLIERL LADGNDVDEV VWGTIMPVVT ANVTNQSQVM
ALCLDYYLGD EGNSHLPELY RLAHEDTPEA DELLMKYMLE GCRLRGTVAV YRQAASNQVI
TDYPPCVPNE SDPASRNPVT NPNIEGSTYE VKIAKGQRVV CNLMTAGRDP AIFEKPNEVR
TDRPLESYVH FGLGPHWCAG KEISRIAQTS MFKQLVGLKN LRRAPGGRGK LKNFPASPWQ
GQVGLPTEGQ NGHGPVKPWL GLRSFMTADQ SSYWPVPTTL RVQWDD
//
