ID   CP4D1_DROSI             Reviewed;         512 AA.
AC   O16805;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cytochrome P450 4d1;
DE            EC=1.14.-.-;
DE   AltName: Full=CYPIVD1;
GN   Name=Cyp4d1;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CAS-31;
RA   Phillips K.S., Begun D.J., Aquadro C.F.;
RT   "Evidence for non-neutral evolution around the cytochrome p450 gene cluster
RT   on the Drosophila melanogaster X chromosome.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the metabolism of insect hormones and in the
CC       breakdown of synthetic insecticides. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF017005; AAB71168.1; -; Genomic_DNA.
DR   AlphaFoldDB; O16805; -.
DR   SMR; O16805; -.
DR   ChiTaRS; Cyp4d1; fly.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   Gene3D; 1.10.630.10; -; 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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN           1..512
FT                   /note="Cytochrome P450 4d1"
FT                   /id="PRO_0000051833"
FT   BINDING         316
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         456
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:0000250"
SQ   SEQUENCE   512 AA;  58624 MW;  D61B214D36208F2F CRC64;
     MFLVIGAILA GALFVGLLLY QLKFKRLIDL ISYMPGPPVL PLVGHGHHFI GKPPHEMVKK
     IFEFMETYSK DQVLKVWLGP ELNVLMGNPK DVEVVLGTLR FNDKAGEYKA LEPWLKEGLL
     VSRGRKWHKR RKIITPAFHF KILDQFVDVF EKGSRDLLRN MEQDRLKHGD SGFSLYDWIN
     LCTMDTICET AMGVSINAQS NADSEYVQAV KTISMVLHKR MFNILYRFDL TYMLTPLARA
     EKKALNVLHQ FTEKIIVQRR EELIREGSSQ ESSKDDADVG AKRKMAFLDI LLQSTVDERP
     LSNLDIREEV DTFMFEGHDT TSSALMFFFY NIATHPEAQK KCFEEIRSVV GNDKSTPVSY
     ELLNQLHYVD LCVKETLRMY PSVPLLGRKV LEDCEINGKL IPAGTNIGIS PLYLGRREEL
     FSEPNSFKPE RFDVVTTAEK LNPYAYIPFS AGPRNCIGQK FAMLEIKAIV ANVLRHYEVD
     FVGDSSEPPV LIAELILRTK DPLMFKVRER VY