ID N1Q8V2_PSEFD Unreviewed; 1167 AA.
AC N1Q8V2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Linoleate diol synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MYCFIDRAFT_48406 {ECO:0000313|EMBL:EME88206.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME88206.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME88206.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME88206.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; KB446555; EME88206.1; -; Genomic_DNA.
DR RefSeq; XP_007920036.1; XM_007921845.1.
DR AlphaFoldDB; N1Q8V2; -.
DR GeneID; 19339823; -.
DR KEGG; pfj:MYCFIDRAFT_48406; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000016932; 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:UP000016932}.
FT BINDING 407
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 1167 AA; 131584 MW; 4FA5C74E96B05076 CRC64;
MSHSAKSNCV KMPLDPELST LDRYRQSVGQ SLTSLKTLLN AVRAPLPKDT GDGTYLPQAD
NETVLGEIND VIRDLARQDI KDIAGLVETV KGAALDKPLD DRKYLMETMV RVASKLPTDD
LQKKITETLI ITLWNDLEHP PQTLLSDEFQ FRQPDGSNNS YKYPDIGKAG MPYARTVAPK
TKQAGVLPDP GILFDSVLAR KSPKGELHPN RISSMLFYLA SIIIHDIFRT DHRDFTKSNT
SSYLDLAPLY GSNWEEQKKM RTFKNGMIKP DCFSETRLLG LPPGVGAILI CFNRYHNYVV
QQLAAINEDG RFTEDAEKPA MVERYTNKEG KKDTINKRDD DLFQTARLIT CGLYINIILI
DYVRTILNLN RTDSNWQLNP RVEVQDGPPM GTGNQCSAEF NLVYRWHSAI SERDDYWTQE
LFKEMFPGVE PSKVAEPQNV GMFLGKLAED QMKIQKLDPT ERPFPALKAE QEKMPRKKDG
PFKGNYDDDD LADLLTSSIE DCANAMGPQQ VPTIMKAIET LGINQARTWR CATLNEMRKH
FKLKPHEKFS DITENEEVAT ALKHLYDSPD QVELYPGLVV EDAKDPVLPG SGLCPSYTVS
RGVLSDAVAL VRGDRFYTSA YTPALLTNWG YQEAHYDLAI DNGCVFYKLF LRALPNSFDP
MSVYVHYPLT IPSETRTILK GLKKDHLYNF DRPQESHHPV VLFSAEAAKK VTEDQETFHV
TWGPAMEFLM GPKAKNFMLA GDGPENAASR KIMEKPMYQG ASSRSIPQGN EKWLRAVRDF
YELKTTELLK QKSYKLAGMR YVDIIRDVSN MAHVAFGAEL FSIPLKTEDF PHGIFTEQQL
YLIMAAVFIC VFFDLDPPKS FPLRVKAREA CQTLGKIMAL QVESVKRFGK LSETLIDAVM
PNEGPLKEYG VHMIAQLCKA NPDLSVDDLV WGNIMGTAGG MIPNQGQLFG QALDYFFTNE
GHKYWSDIQK LAKQDTLEAD DKLMHYLMEA ARLSGETGAF RYATKDVTIV DDTGLENLPI
GDKGKITHHI KQGDIVMVNF KAASRDARLF PNPDQLDLNR PLDSYLMLGH GAHQCLGLPM
TRVALTTMLK VIARLDGLEP MPVSVGKQSG PHCVKKVVKE FIPGDRAYLP ESWHYHLYLT
EDWDQYFPFP TSLKLRFKGE VPNVKAA
//