ID   CP52P_CANTR             Reviewed;         505 AA.
AC   P30612;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Cytochrome P450 52C1;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK7;
DE   AltName: Full=CYPLIIC1;
GN   Name=CYP52C1;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX   PubMed=1457045; DOI=10.1089/dna.1992.11.767;
RA   Seghezzi W., Meili C., Ruffiner R., Kuenzi R., Sanglard D., Fiechter A.;
RT   "Identification and characterization of additional members of the
RT   cytochrome P450 multigene family CYP52 of Candida tropicalis.";
RL   DNA Cell Biol. 11:767-780(1992).
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}. Membrane; Single-pass
CC       membrane protein.
CC   -!- INDUCTION: By various alkanes.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; Z13014; CAA78358.1; -; Genomic_DNA.
DR   PIR; S22976; S22976.
DR   AlphaFoldDB; P30612; -.
DR   SMR; P30612; -.
DR   VEuPathDB; FungiDB:CTMYA2_060220; -.
DR   VEuPathDB; FungiDB:CTRG_04959; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..505
FT                   /note="Cytochrome P450 52C1"
FT                   /id="PRO_0000052033"
FT   TRANSMEM        4..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         453
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   505 AA;  58094 MW;  1BE07934160D0FAD CRC64;
     MYQLFCFLAG IIVVYKAAQY YKRRTLVTKF HCKPARISPN KSWLEYLGIA SVVHADEMIR
     KGGLYSEIDG RFKSLDVSTF KSITLGKTTY VTKDIENIRH ILSATEMNSW NLGARPIALR
     PFIGDGIFAS EGQSWKHSRI MLRPVFAKEH VKQITSMEPY VQLLIKIIKN HEGEPLEFQT
     LAHLFTIDYS TDFLLGESCD SLKDFLGEES NSTLDTSLRL AFASQFNKTQ QQMTIRFMLG
     KLAFLMYPKS FQYSIQMQKD FVDVYIDRVV GMSEEELNNH PKSYVLLYQL ARQTKNRDIL
     QDELMSILLA GRDTTASLLT FLFFELSHHP EVFNKLKEEI ERHFPDVESV TFGTIQRCDY
     LQWCINETMR LHPSVPFNFR TAANDTVIPR GGGKSCTDPI LVHKGEQVLF SFYSVNREEK
     YFGTNTDKFA PERWSESLRR TEFIPFSAGP RACLGQQLPR VEASYVTIRL LQTFHGLHNA
     SKQYPPNRVV AATMRLTDGC NVCFI