ID A0A0F0I2K4_ASPPU Unreviewed; 533 AA.
AC A0A0F0I2K4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KJK61979.1};
GN ORFNames=P875_00086502 {ECO:0000313|EMBL:KJK61979.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK61979.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK61979.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602402-1};
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:KJK61979.1}.
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DR EMBL; JZEE01000651; KJK61979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0I2K4; -.
DR STRING; 1403190.A0A0F0I2K4; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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: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 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; IPR002402; Cyt_P450_E_grp-II.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24287; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR24287:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00464; EP450II.
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|PIRSR:PIRSR602402-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|PIRSR:PIRSR602402-1, ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602402-1,
KW 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:UP000033540};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 478
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602402-1"
SQ SEQUENCE 533 AA; 60723 MW; D82E7AFB3ACF302A CRC64;
MMIPQQWSFS TVLPAIFGIC IFRWILISIL HTQRAQRMGC KPAFVRRSKL PFGIDILKRY
IDTTRQQILQ NDEVVLYEEL GQHPTWNQNI LGTWHHVTVD PKNVQAMLAT QFKDFELGSS
RLNLFGPVIG KGIFTTDGKE WQHSRSLLRP QFARGQVANL ELEERHVQHL LDRLPVQHDS
WTDVVDLGPL FFNLTLDSAT EFLFGQSVNS QVASAKGNQS HESGAAVPAG LPDGLSFGHA
FDRANTVVAL RSWLMDLYFL YSPAEFRKDC AEIHRFARYY VNLALAEESK SGDNKRSPEN
PTDSGYVFLR ELVKETKDPE ELRTQLLNIL LAGRDTTAGL LGWTFYLLSR HVDVYEKLRA
VVIETFGEFS HNTSITFESL KSCSYLQHVL SEVLRLHPPV PENGRRAVRN TTLPRGGGAD
GTSPIYIRAG EEVAYNVHVM HRRKDLWGED AEEFRPERWT GHKPGWEFLP FNGGPRICLG
QQFALTEAGY IIVRMLQRFD KVENMDKSTV VKHKYTTTTA PVQVLVRLYS TSH
//
