ID A0A135TV05_9PEZI Unreviewed; 1106 AA.
AC A0A135TV05;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Linoleate diol synthase {ECO:0000313|EMBL:KXH52000.1};
GN ORFNames=CSIM01_07819 {ECO:0000313|EMBL:KXH52000.1};
OS Colletotrichum simmondsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH52000.1, ECO:0000313|Proteomes:UP000070328};
RN [1] {ECO:0000313|EMBL:KXH52000.1, ECO:0000313|Proteomes:UP000070328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS122122 {ECO:0000313|EMBL:KXH52000.1,
RC ECO:0000313|Proteomes:UP000070328};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum simmondsii CBS122122.";
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:KXH52000.1}.
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DR EMBL; JFBX01000049; KXH52000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TV05; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000070328; 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: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:SF13; LINOLEATE 10R-LIPOXYGENASE; 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}.
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 414
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 1106 AA; 124006 MW; 9629993DC00CD06C CRC64;
MKTSRNGSNS SAGADTYKPT TTGPSMKNPH PGPSRADPRY GSHDVKKKGF SDIRQASKRP
LPTQNGDGTY PSDLTRPTMV QNLKALQAAD LKTLVQIIKS KIKREKIQDD KTMIMERTIQ
IVAKLPHNSR LREQLTNTFI EELWGSLDHP PMLYMGDEYK YRQADGSYNN PMLPRLGAAG
GPYARSVKPR IVTLGAMPDP GLIFDAVMGR TSYKKHPNNV SSILWYWATI IIHDLFWTDF
KDMTKSKTSA YLDLSPLYGS NQEMQNSIRT FKDGKLKADS FADKRLIGMP PGVCVLLIMF
NRFHNHVAEN LAAINEGGRF TPPSKDLNEE QTAAALKKYD EDLFQTARLV TSGLYINITL
VDYVRNIVNL NRTNTTWTLD PRQEAGIDAG TPDGAEAGTG NVNSAEFNLC YRWHSCISDK
DDKWIQKFYG KLLGNKGQMS PQEMACVFGQ FEKSIPDDPG MRTFAEYERG ADGKFDDDDL
VDCISSAIED CAGAFGARNV PQVMRPVEIM GILQGRKWNV AGLNEFRKHF GLKPHETFED
INSDPAVADQ LRNLYQHPDY VELYPGLVAE EAKTPLTPGV GIAPTYTISR VVLSDAVCLV
RGDRYYTTDY NPRHLTQWGY KEVEYDLNVN HGCVFYKLFL RAFPNHFKGN SVYAHYPMVI
PPENQQILTD LGRVNQFDFE RPKPIPTRTN ITSFGGAKYV LDSQSRFKVT WDEGLSFLMG
KGGGRFMLSG DTDFHTGQKK CMSAQLYQDD WSSHVKRFYA EITEQLLREK SYKLAGQTHV
DIIRDVGNIA HVHFAARVFN LPLKTHKNPK GVFTEQEMYQ ILAVIFVCIF FDIDPAKSFP
LRQAAKEAAQ SLGKLIETNV KITTKTGLRG IFTGSADKQD PLALYGTNVI KGLDKAGLST
YDIAWSQILP TSGAMVPNQA QVFAQAVDYY LSPPGSKHLD QIHAVAKAPS TKESDAVLLG
YAMEGIRLAG TFGSYREAAQ DDVIVEDGGR EVPVRRGDKI FVSFVSAAKD ANHFPHPEEV
NPRRPIDSYI HYGLGPHSCL GRDVSQVALT EMFRVLFRKT NVRRVPGPQG LLKKVPRPGG
FFVYLKEDWG QIWPFPVTMK VMWDDE
//