ID   S8BBI9_PENO1            Unreviewed;       506 AA.
AC   S8BBI9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PDE_07207 {ECO:0000313|EMBL:EPS32247.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS32247.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS32247.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
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DR   EMBL; KB644414; EPS32247.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8BBI9; -.
DR   STRING; 933388.S8BBI9; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_5_11_1; -.
DR   OrthoDB; 2954533at2759; -.
DR   PhylomeDB; S8BBI9; -.
DR   Proteomes; UP000019376; 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   GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   CDD; cd11069; CYP_FUM15-like; 1.
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; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF227; P450, PUTATIVE (EUROFUNG)-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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019376}.
SQ   SEQUENCE   506 AA;  56664 MW;  996A073D18B9BCDF CRC64;
     MFRCSFIGSF ALLVIWKLYL WPIWFSPLRN LPEPPGGQLL SGHTRLVPNE RSGMPLQEWI
     NQVPNSGLIR YRMRFNKEVI FVTNPKGLSE VLVQKSYEFA KPAKLRLGLG RILGVGLIVA
     EGNQHKKQRK LLMPAFLHRH IKDLYPIFWD KSVALAQVLR ENISLSRDDS THVFDVGDWL
     ARATLDILGA AGLGEEFDTL HHPDNEICSA YRNVFELKPP QGTLAMGVFL MREALVKMLG
     LSRKDSISLA TKTLTDVARR LIARKRSKMQ AHDSKEPGRD IISVALSSDS FTDPMLENHL
     LTFLAAGHET TATSMTWALY ALCIYPDVQR RLRDEVRQFL PQYFDHATAP PMKAELLDSL
     PYLHAVCNEV FRVYPPAGLT RRVAVQNTSI LGQFIPAGTE IVISPRAVNV SRDLWGPDAA
     TFNPDRWMKP NQANTGGGLT NFSFMTFLHG PRSCIGQGFA RGEFASLLAA LVGSFEMSLA
     QDPDIEIETG LTSRPKGGLL VEFRKI
//