ID   C12B1_DROAC             Reviewed;         532 AA.
AC   O44220;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Cytochrome P450 12b1, mitochondrial;
DE            EC=1.14.-.-;
DE   AltName: Full=CYPXIIB1;
DE   Flags: Precursor;
GN   Name=Cyp12b1;
OS   Drosophila acanthoptera (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=51166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=A584.2;
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; U78485; AAB88725.1; -; mRNA.
DR   AlphaFoldDB; O44220; -.
DR   SMR; O44220; -.
DR   FlyBase; FBgn0022933; Daca\Cyp12b1.
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           ?..532
FT                   /note="Cytochrome P450 12b1, mitochondrial"
FT                   /id="PRO_0000003610"
FT   BINDING         480
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   532 AA;  62031 MW;  2E94D7FC66FDF569 CRC64;
     MWKFAIHSQQ PFCWQQLCNR RHLYVGNVQQ QTHLELLDAA PTRSDDEWLQ AKPYEKVPGP
     GTWQVLSYFL PGGKQYNTNL IQMNRRMREW YGDIYRFPGL MGKQDVIFTY NPNDFELTYR
     NEGVWPIRIG LESFTYYRKV HRPEVFGSIG GLVSEQGKDW AHIRNKVNPV QMRVQNVRQN
     LPQIDQISRE FVDKLDTLRD PVTHILNDNF HEQLKMWAFE SISFVALNTR MGLLSDRPDP
     NAARLAEHMT DFFNYSFKYD VQPSIWPYYK TPGFKKFLQT YDKITEITTA YIDEAIKRFE
     IEKDSGNECV LQQLLSLNKK VAVVMAMYML MAGIDTTSSA FVTILYHLAR NPHKQRQLHR
     ERRRILPDSD EPLTPENTKN MPYLRACIKE CMRITSITPG NFRIATKDLV LSGYRVPRGE
     GVLMGVLELS NSEKYFGQSG QFMPERWLKA DTDPDVKACP AARSRNPFVY LAFGFGPRTC
     IGKRIAELEM ETLLTRLLRR YQVSWLAEMP LQYESNIILS PHGIYVQVRA AC