ID A0A1V6QYM2_9EURO Unreviewed; 491 AA.
AC A0A1V6QYM2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENSOL_c027G10231 {ECO:0000313|EMBL:OQD94289.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD94289.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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:OQD94289.1}.
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DR EMBL; MDYO01000027; OQD94289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QYM2; -.
DR STRING; 60172.A0A1V6QYM2; -.
DR OrthoDB; 3184603at2759; -.
DR Proteomes; UP000191612; 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:UniProtKB-KW.
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; cd11062; CYP58-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF157; N-ACETYLTRYPTOPHAN 6-HYDROXYLASE IVOC-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000191612}.
SQ SEQUENCE 491 AA; 55645 MW; D407723D98BADF6E CRC64;
MLLLWLGFLS FVFGVVIYRL QFHPLSKFPG PKLAALTSLY EFYYNVVLGG RYLWEIERMH
EQYGPIVRIT PHELHVADPD FYTEIYAGPT RRRDKDPRLV RLAGQPMSMF ATVDHSLHSS
RRSILSNYFS KKSIAGLEDM IQRKVQKLVK RLNLACDQGT IVQLDAASSA LTADIISEYA
HGVSLDYLDD VNFNNEVADS ILSLASVVHV LKFFPFLLDL SKYIPDEVLG KLWPHAANIL
RLQKLVRAQA DVALQNEGKV DGQVTMFGAL CDPSLPAQER TLDRLQDEGF SLIGGGTETT
TGTLKICMFH LLNDKSLLLK LREELEQSPS STWAELEKLP YMRGVINEGL RLSGVITRLP
RRAPDEALKY KQWTIPPNSL MSTSTHFVHT NKDLFPDPHT FDPERWIRAE AAGERLEHMI
VTFSKGSRQC LGNHLALAEL YLVISMMVRK FDMDLYGVTA DNIVTHREYG FGVPKARGDG
FRVRIKRVPN P
//
