ID A0A0A2K8Y8_PENEN Unreviewed; 423 AA.
AC A0A0A2K8Y8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Cytochrome P450, E-class, CYP52 {ECO:0000313|EMBL:KGO57337.1};
GN ORFNames=PEX2_000120 {ECO:0000313|EMBL:KGO57337.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO57337.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO57337.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO57337.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO57337.1}.
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DR EMBL; JQFZ01000147; KGO57337.1; -; Genomic_DNA.
DR RefSeq; XP_016599005.1; XM_016737290.1.
DR AlphaFoldDB; A0A0A2K8Y8; -.
DR STRING; 27334.A0A0A2K8Y8; -.
DR GeneID; 27672709; -.
DR HOGENOM; CLU_001570_27_0_1; -.
DR OrthoDB; 4950799at2759; -.
DR PhylomeDB; A0A0A2K8Y8; -.
DR Proteomes; UP000030143; 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:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of 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; cd11063; CYP52; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002974; Cyt_P450_E_CYP52_ascomycetes.
DR InterPro; IPR047146; Cyt_P450_E_CYP52_fungi.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24287:SF18; CYTOCHROME P450 MONOOXYGENASE APDE-RELATED; 1.
DR PANTHER; PTHR24287; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR01239; EP450IICYP52.
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:UP000030143}.
SQ SEQUENCE 423 AA; 47644 MW; EB93DD984B039399 CRC64;
MTFKLFGNQG YLTADPKNVE SILSTNFEDW CLGSRRPGLM PMLGEGIFTQ DGRPWKHSRE
LLRRQFVRIH RQDSKIFDEH VEELISNLRS ATASGVVDLQ PHLFRFTLAT TTALIFGEPV
FALPGAETDT FEKAFDYASY ISAIRLRLAD LEWIWKPAKF RAACDVVKEY ASHFVQLALD
DMEKNGEEAA SERHAFILEL YKEMQDKVLV RDQLVHVLIA GRDTTACLMS WAFFLLVRHP
ETLAKLRSEI QDVTGGSHEL SRAKISKMTY LRCVINESQR LYPQLPVNVR VAAKTTFLPS
GGGPDGKSPV LIPKNTGVGY SVYHMHRLKS VYGEDANSFR PERWLGPELD GIGWGFMPFH
GGPRICLGKE FALTEASHAI IRIIQTFPEL RLPPETPIVP PGEEKQALTI VVMSAEGCKV
LLD
//
