ID A0A0F0I8S9_ASPPU Unreviewed; 550 AA.
AC A0A0F0I8S9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KJK63536.1};
GN ORFNames=P875_00065001 {ECO:0000313|EMBL:KJK63536.1};
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:KJK63536.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK63536.1, 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:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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:KJK63536.1}.
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DR EMBL; JZEE01000553; KJK63536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0I8S9; -.
DR STRING; 1403190.A0A0F0I8S9; -.
DR Proteomes; UP000033540; 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 CDD; cd00302; cytochrome_P450; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF87; CYTOCHROME P450 MONOOXYGENASE ALND-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT BINDING 497
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:PIRSR602403-1"
SQ SEQUENCE 550 AA; 61464 MW; 58EF69ED1F46FA65 CRC64;
MKCQFYLVGD DIATAQSIDV ESRWKFDDLQ RAVGGVFHVA LPTGISFHTS ENETLSSVAD
IISASSSPIG LRIDGNAVQT PQGPPGLPLV GSFYEIFPDH LGNHYRLFRK YGPVIKTTNM
GKTTYLTDDP QVASVCLAES AYMTKKINEN HPLWGVKDNT AIFIGDTETE NWRLAHKYLP
PAMGPKAVRH YTGLMQNCAR KSLPVFDELD GRDESWNVYQ YMVKLASQTI GSFSLGKDFG
HFDSVDSPLH PIVTNIASLL SLNKKITARG EWYRHLPFGD PARLRHVQHT IYTLLQEAID
EVAGSGIADA PMNEAALSAS CVVDYLLHAV DDKGEHFPQG LILANMLIVT GAGFTTTSAL
LSWLLYCLVT YEGTQDRLYA ELVEHGIVGP SGERNQTAWT PDLAHSLPYL DKFVKETQRL
HNASFQPGRT TKTDVVLPGG YRLPPDSVIV PALYAIHTNP KTWRDPFRFD PDRWDTEEVK
GRHRCAYIPF ATGPRGCIGF NFALLEVKVL LAELVSRYEF VRDGLEAIDY DPEFQLIRPL
NFYVRAKRRV
//
