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Database: UniProt
Entry: A0A316UX08_9BASI
LinkDB: A0A316UX08_9BASI
Original site: A0A316UX08_9BASI 
ID   A0A316UX08_9BASI        Unreviewed;       494 AA.
AC   A0A316UX08;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:PWN27655.1};
GN   ORFNames=BDZ90DRAFT_232072 {ECO:0000313|EMBL:PWN27655.1};
OS   Jaminaea rosea.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Jaminaea.
OX   NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN27655.1, ECO:0000313|Proteomes:UP000245884};
RN   [1] {ECO:0000313|EMBL:PWN27655.1, ECO:0000313|Proteomes:UP000245884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN27655.1,
RC   ECO:0000313|Proteomes:UP000245884};
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
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DR   EMBL; KZ819667; PWN27655.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316UX08; -.
DR   STRING; 1569628.A0A316UX08; -.
DR   OrthoDB; 2900138at2759; -.
DR   Proteomes; UP000245884; 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: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   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR46300:SF2; CYTOCHROME P450 MONOOXYGENASE ALNH-RELATED; 1.
DR   PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   4: Predicted;
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245884}.
SQ   SEQUENCE   494 AA;  55625 MW;  6E83390B22A09B0C CRC64;
     MSLLLYGFAF VGLLLYSIWP KRRLAPGPPR LPIVGSLPFI DQSKHLLEQA PAWREKYGGV
     VQVSLGMADW LLITKVADAR QLLYGTAVED RPRLMLYHDE IHPERWLGPA AKADEWILAT
     RRVTGQLVRT VGDHGGEHAA KMMLEWLEFH LKEQPDFERT LWHFAVANAL ESAYGIQLES
     ASQAAEFDEL QDLIDTGRHM MTAFDPQSEP TVFFPFVEHL NPSRTRTIKA RGAAMYAEWE
     TRAKRLGGKV REMGKNAKAS QFDLAGRDKE YSMTEDELDY QGALLLVGTL DTVYHTSVLA
     AACFAYLGDA QQQIREEVDA LSAQGAPASQ SPKLVAFLRE TLRLYPFAAT GFPRQTSKPL
     PLPGRSDKVL PVGTVLVPLT MTLARDQEYW GPDAEEHNYR RFMEDDTLKA QPFPVFGYGY
     GRRACPGYRL AEVMMANAIG GLLSRYELSF EGRDSGETDA TATLDETLRI KLRGNVFMMD
     LPRCRTTRRR DCPM
//
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