ID   CP52Q_CANMA             Reviewed;         510 AA.
AC   Q12587;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cytochrome P450 52C2;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK6-A;
DE   AltName: Full=CYPLIIC2;
GN   Name=CYP52C2;
OS   Candida maltosa (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977;
RX   PubMed=7865134; DOI=10.1089/dna.1995.14.163;
RA   Ohkuma M., Muraoka S., Tanimoto T., Fujii M., Ohta A., Takagi M.;
RT   "CYP52 (cytochrome P450alk) multigene family in Candida maltosa:
RT   identification and characterization of eight members.";
RL   DNA Cell Biol. 14:163-173(1995).
CC   -!- FUNCTION: Together with an NADPH cytochrome P450 the enzyme system
CC       catalyzes the terminal hydroxylation as the first step in the
CC       assimilation of alkanes and fatty acids.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC   -!- INDUCTION: By various alkanes.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D12718; BAA02212.1; -; Genomic_DNA.
DR   PIR; JS0724; JS0724.
DR   AlphaFoldDB; Q12587; -.
DR   SMR; Q12587; -.
DR   GO; GO:0016020; C: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: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   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002974; Cyt_P450_E_CYP52.
DR   InterPro; IPR002402; Cyt_P450_E_grp-II.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01239; EP450IICYP52.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..510
FT                   /note="Cytochrome P450 52C2"
FT                   /id="PRO_0000052034"
FT   BINDING         458
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   510 AA;  58113 MW;  2AD3F6B48AC596B8 CRC64;
     MIDALYILIV ALVIYKTAQF VHRKSLEKKH HCQPVKQIPL VSILSGLGFD MFFKDTAEMT
     KNGGLHKKLQ QMLESLQTTT FRSRMLTGSQ IVTMEPENER TMCSSAHMKD WTIGYRPFAL
     KPLLGDGIFS SEGESWKHSR IMLRPIFAKE HIKQITAMEP YMLLLIEIIK SSSANEGPVD
     LQPLFHAFTI DYASDFLFGE SCDVLKENLG GKSTSGMDAQ VKRDFASVFN DVQNYLTKRM
     MLGPLAFLVS SKDFHDGIKK QHEFVSYFVQ KAISMSDEEL NDESKNYVFL YQLAKQTKDA
     KVLQDELLSI LLAGRNTTAS LLSFLFFELS HHENVWTTLK EVVDQSFPDV ESITFETIQN
     CDYLRWCLFE SLRVNPSVPF NSRTANKDTI LPRGGGEDCS HPILVKKGDQ VLFPLYASNR
     QEKYFGRKPE EFIPERWRDL PKTGGPAFMP FSTGPRMCLG QQFALIEASY VTIRLVQTFS
     KLKSHSLEYA PKRLVAATIR LIDGCFVSFE