ID   CP52F_CANTR             Reviewed;         524 AA.
AC   P30608;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Cytochrome P450 52A6;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK3;
DE   AltName: Full=CYPLIIA6;
GN   Name=CYP52A6;
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       hexadecane.
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; Z13010; CAA78354.1; -; Genomic_DNA.
DR   PIR; S22972; S22972.
DR   AlphaFoldDB; P30608; -.
DR   SMR; P30608; -.
DR   PRIDE; P30608; -.
DR   VEuPathDB; FungiDB:CTMYA2_045880; -.
DR   VEuPathDB; FungiDB:CTRG_02725; -.
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..524
FT                   /note="Cytochrome P450 52A6"
FT                   /id="PRO_0000052024"
FT   TRANSMEM        17..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         472
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   524 AA;  59928 MW;  3128E3F5B2135749 CRC64;
     MATQEIIDSA LPYLTKWYTV ITLAALVFLI SSNIKNYVKA KKLKCRDPPY FKGAGWTGIS
     PLIEIIKVKG NGRLARFWPI KTFDDYPNHT FYMSIIGALK IVLTVIQENI KAVLATQFTD
     FSLGTRHAHF YPLLGDGIFT LDGEGWKHSR AMLRPQFARD QIGHVKALEP HIQILAKQIK
     LNKGKTFDIQ ELFFRFTVDT ATEFLFGESV HSLYDEKLGI PTPNEIPGRD NFATAFNTSQ
     HYLATRTYSQ TFYFLTNPKE FRDCNAKVHY LAKYFVNKAL NFTPEEIEEK SKSGYVFLYE
     LVKQTRDPKV LQDQLLNIMV AGRDTTAGLL SFAMFELARH PEIWSKLREE IEVNFGVGEE
     SRVEEITFES LKRCEYLKAI LNETLRMYPS VPVNSRTATR DTTLPRGGGP NGTDPIFIPK
     GSTVAYIVYK THRLEEYYGK DADDFRPERW FEPSTKKLGW AYVPFNGGPR ICLGQQFALT
     EASYVITRLV QMFETVSSPP DVEYPPPKCI HLTMSHDDGV FVKM