ID   CP52G_CANTR             Reviewed;         507 AA.
AC   P30609;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cytochrome P450 52A7;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK4;
DE   AltName: Full=CYPLIIA7;
GN   Name=CYP52A7;
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. Preferentially hydroxylates
CC       lauric acid.
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; Z13011; CAA78355.1; -; Genomic_DNA.
DR   PIR; S22973; S22973.
DR   AlphaFoldDB; P30609; -.
DR   SMR; P30609; -.
DR   VEuPathDB; FungiDB:CTMYA2_002860; -.
DR   VEuPathDB; FungiDB:CTRG_03120; -.
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..507
FT                   /note="Cytochrome P450 52A7"
FT                   /id="PRO_0000052025"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
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   507 AA;  58671 MW;  34B23DED3D1E5C87 CRC64;
     MIEQVLHYWY YVLPAFIIFH WIVSAIHTNS LRRKLGAKPF THTQLDGFYG FKFGRDFLKA
     KRIGRQVDLI NSRFPDDIDT FSSYTFGNHV IFTRDPENIK ALLATQFNDF SLGGRIKFFK
     PLLGYGIFTL DGEGWKHSRA MLRPQFAREQ LPMSPSLEPH FNVKAYPQEQ RWVFDIQELF
     FRFTVDSATE FLFGESVNSL KSASIGCDEE TELEERKKFA EAFNKAQEYI STRVALQQLY
     WFVNNSEFKE CNEIVHKFTN YYVQKALDAT PEELEKQSGY VFLYELVKQT RDPNVLRDHH
     SISLLAGRDT TAGLLSFAVF ELARNPHIWA KLREDVESQF GLGEESRIEE ITFESLKRCE
     YLKAVMNETL RLHPSVPRNA RFALKDTTLP RGGGPDGKDP ILVRKMSCSI FISGTQIDPK
     HYGKDAKLFR PERWFESSTR NLGWAYLPFN GGPRICLGQQ FALTEAGYIL VRLAQSFDTL
     ELKPDTEYLT KISHLTMCLF GAFVKMD