ID   CP4E5_DROMT             Reviewed;         522 AA.
AC   O44221;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Cytochrome P450 4e5, mitochondrial;
DE            EC=1.14.-.-;
DE   AltName: Full=CYPIVE5;
DE   Flags: Precursor;
GN   Name=Cyp4e5;
OS   Drosophila mettleri (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7228;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9304797; DOI=10.1016/s0965-1748(97)00035-0;
RA   Danielson P.B., Fogleman J.C.;
RT   "Isolation and sequence analysis of cytochrome P450 12B1: the first
RT   mitochondrial insect P450 with homology to 1 alpha,25 dihydroxy-D3 24-
RT   hydroxylase.";
RL   Insect Biochem. Mol. Biol. 27:595-604(1997).
CC   -!- FUNCTION: Probably involved in steroid hormones biosynthesis.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U78486; AAC27534.1; -; mRNA.
DR   AlphaFoldDB; O44221; -.
DR   SMR; O44221; -.
DR   FlyBase; FBgn0023312; Dmet\Cyp4e5.
DR   GO; GO:0005739; C:mitochondrion; 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   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           ?..522
FT                   /note="Cytochrome P450 4e5, mitochondrial"
FT                   /id="PRO_0000003581"
FT   BINDING         307
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         443
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:0000255"
SQ   SEQUENCE   522 AA;  60609 MW;  E7BA14352E6B47C2 CRC64;
     MWFIVYILLA LPIMLFVFLS CEWPKRNDAE QIEWSSGVPF LGNAHQMGKT PAEILNTFFE
     FWHKYNKDNF RIWIGYYANI LVSNPKHLEV IMNSTTLIEK LDIYDMLHPW LGEGLLTSKG
     SKWHKHRKMI TPTFHFNILQ DFHQVMNENS AKFIKRLKEV SAGDNIIDFQ DETHYLTLDA
     ICDTAMGVTI NAIEKRDTVD VVKAFKDMCH IINMRAFRPL QRSDFLYRFS PEYATYAKTL
     KTLKDFTNDI IAKRIKVHRT AAAKTNQEGS EFSRKKMLPD TLLSATIDGR PLNQQEIYEE
     VSTFMFEGHD TTTSGVAFAG YILSRFPEEQ RKLYEEQQAV MGNELNRDAT FQEISAMKYL
     DLFIKEAQRV YPSVPFIGRY TDKDYNIHGT IMPKGTTLNL GIIVLGYDDR VFEEPHRFYP
     ERFEKQKPGP FEYVPFSAGP RNCIGQKFAL LELKTVISKL VRTFEVLPAV DELVSKDGNL
     NTYVGLPKEE KERKERMGYK YDPILSAVLT LKSENGLHLR LR