ID A0A010RKV6_9PEZI Unreviewed; 1185 AA.
AC A0A010RKV6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Linoleate diol synthase {ECO:0000313|EMBL:EXF78514.1};
GN ORFNames=CFIO01_09729 {ECO:0000313|EMBL:EXF78514.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF78514.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF78514.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF78514.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXF78514.1}.
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DR EMBL; JARH01000630; EXF78514.1; -; Genomic_DNA.
DR RefSeq; XP_007597829.1; XM_007597767.1.
DR AlphaFoldDB; A0A010RKV6; -.
DR KEGG; cfj:CFIO01_09729; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000020467; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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:InterPro.
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; 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; 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 Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467}.
FT REGION 299..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 431
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 1185 AA; 133481 MW; CE41B05D5BAB1D6A CRC64;
MSQAQEQFPK HQPLLTEVSE KLAAARNLVH KSISAVPPHP EPVPGTAAQQ AEPTNLLQDI
KKLGFQDFET LAEFGITAVQ GKIDDNELLL EHLIQLFAKL PRGTVKGKKL EYGLINQLWN
GIDHPPMTTL DEKFKYRAAD GSNNNIHSPA MGAAGTAYAR SAPAITYQTP NQPDPSLLFD
MLFARGEEFK PHPNKISSFL FYLATIITHD IFQTDGLSGI NRTSSYLDLS PLYGRNQEEQ
DQVRTKLDGR LKPDSFSSKR VLGFPPGVGV LLMMFNRFHN YIVTQLASIN ENNRFNRPTG
DAIDPKAEAP KKPAEPEGAV PVGHPKYLDY TESPAYKEYT NTPEYKQWAN WTAWVKFDND
LFQTARLITC GLYVSIVLRD YVRTILNMNR SPSSWALDPR TNEGKSILRA ETPEGTGNQV
SVEFNLIYRW HCTISPKDAK WTEKAFREQL KIKGVTKDIK DYTLMEFGHA VRDWEGRISN
DPLERDFAGL KRGKDSAYRE EDLVKIFKES VEDVAGSYGA NRIPEIMKPI EVLGMMNARK
WNVATLNEFR DHFGLTRHPT FEDINPDPEV VKKLRYLYGT PDQVELYPGL VAEKAKEPMS
PGSGLCGGFT MTRAILSDAV ALVRGDRFYT IDYTPKNLTN WGFNQCSYDH NVDQSHVLYK
LVFRAFPNSF EQNSVYAHFP LTVPSENKKI LEDINRAYLY SWKEPVTKRS MIPIFSHKAV
SEILYNQTDF KVVWGDAIRH LVAQPGKEHG KDFCLAGDGK ANTQNRTLVR KALITGPWEK
EVFKWYTHTT PRLLKQNSFA IRKGVREVDL VRDVINLTNT RFNAALFHLP IKNEDSPWGV
YTDQELYVVV ATLFQSVFLD ADIGNSFKLR TIARELGQGL GKLMSLICLT ISKAGLITDI
VAKIREGESS LPTFGNHLIE RLLADGKDIE EVVWGTIMPV VTANVTNQSQ VMALCIDYYL
GEGHDHLKTL YKLAHEDTPE ADEKLMKYML EGCRLRGTVA VYREAVTTQV ITDYAPCLLD
PNDPTSRTPK INDDIDGTKY EVKIPKGQKV LCNLMTAGRD PTIFEAPNEV RLDRPLESYV
HYGLGPHWCA GKEISRVAQT SLFKQIVGLK GLRRADKTST GNGGRGKLKN MPAGAWPGQV
GLPVGSNQNG AGKKDEPWLG LRTFMTADQS SYWPVPTTMR IEWDE
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