ID A0A316VG83_9BASI Unreviewed; 1057 AA.
AC A0A316VG83;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Linoleate diol synthase {ECO:0000313|EMBL:PWN36592.1};
GN ORFNames=FA14DRAFT_175905 {ECO:0000313|EMBL:PWN36592.1};
OS Meira miltonrushii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN36592.1, ECO:0000313|Proteomes:UP000245771};
RN [1] {ECO:0000313|EMBL:PWN36592.1, ECO:0000313|Proteomes:UP000245771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN36592.1,
RC ECO:0000313|Proteomes:UP000245771};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; KZ819602; PWN36592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316VG83; -.
DR STRING; 1280837.A0A316VG83; -.
DR InParanoid; A0A316VG83; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000245771; 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; 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:UP000245771}.
FT REGION 126..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 369
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 1057 AA; 117588 MW; A2F9EDD375B2A4CC CRC64;
MSQLSKPIRD LITTIAVKPP ANDGDGLDKP EIDSGTLSLL RDLFLTPKRI DDISSFVKLL
LTLASGKPLN DRNLLLENMV SYMQHAPADS EVEQKVADKF ITLLWKDLPH PPVAFLGPEY
RYHSADGSKN NPLQPRLGAA GEPYSRTTSP MHTKSPYMPA PELVFEQLLR RREFTPHSSG
LNRFFFSFAN MVIHEIFRSD PNNKYVNATS SYVELSVLYG DSQDEQDKVR THEQGRIWPD
TFSSARVMMM SPGIIAVAIM FSRHHNYLAQ RLFEVNETGK YKPWDSLTSD KEREWQDNDI
FQLARNINVA FFAKSVLTDY VSGILDTVRA NSDWHLELGK EIRDVQKSRI ERGVGNSVSC
EFNVLYHWHA VLPLSDEKWM NEQFERFCPG VPPEQVTQEQ FYTMAGTLTK EVESISPNAR
TFSNLKRGDD GAFDDTQLGE LIKDCIDETA HSFGARSTPA SFKAIEVAGI LQARNLFQVG
TMNEFREYLY LKRFNSFLEW NPDPKIALAA EKLYGHIDNL ELYPGLMAEE SKPHVPGSGL
QPGHTIGRGI LADAISLVRG DRFLTYDLNA STLTNWGLAQ VEAAPGAYGG HLAHVLYRGL
PNAWGSGNST YSLLPFYTPV AVQKILHDNG TLSRYDVSRP LPSNDLHVLK TRLAVEKALA
DPLTFAVDTT NLDIVTGKDG KIGHRNSLLL HEPAAQKAFF EPGFDANVIQ YFSQTTREKI
QEYSLGVDAT SSTKQLDVIK DIINVVPIYW IAGKVGIPLK TNETPQGLVT VYDLHNTLLT
LAAFVSGVYT PEDAFGLREA AVKQSVHVRK ILEHRFLTTS GARAFVAYMI TRGSQYELST
SAKRVYASLH SDCISMHQAV AGLLAIILPS TVELTTQTGL LLDLFMNPDY AETLERLIEL
ANREDKAACK EFIFLINEGI RLRPATAGVV RKVTENTTVR DGENAVKIKK GEKVLLATSL
ANMDPDAFPN PTRLGPFVDR TEDDLQGVTS QSPVLLSAIV TMLKEIFKLP NIRPAKGVSG
TVVGVSDLIG DVQLRKYIGP HSKEVQGPVS LVAEFDL
//
