ID   CP52T_CANMA             Reviewed;         505 AA.
AC   Q12585;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cytochrome P450 52D1;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK4;
DE   AltName: Full=CYPLIID1;
GN   Name=CYP52D1;
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}. Membrane; Single-pass
CC       membrane protein.
CC   -!- INDUCTION: By N-alkanes.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D12716; BAA02210.1; -; Genomic_DNA.
DR   PIR; JS0722; JS0722.
DR   AlphaFoldDB; Q12585; -.
DR   SMR; Q12585; -.
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 52D1"
FT                   /id="PRO_0000052035"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         446
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;  58388 MW;  A3D59232A6EB7EA8 CRC64;
     MAIFTPELWL ICFAVTVYIF DYIYTKYLMY KLGAKPITHV IDDGFFGFRL PFLITLANNQ
     GRLIEFSVKR FLSSPHQTFM NRAFGIPIIL TRDPVNIKAM LAVQFDEFSL GLRYNQFEPL
     LGNGIFTSDG EPWKHSRIML RPQFIKSQVS HVNRLEPHFN LLQKNITAQT DNYFDIQTLF
     FRFTLDTATE FLFGQSVHSL NDGENSLQFL EAFTKSQAIL ATRANLHELY FLADGIKFRQ
     YNKMVQDFSQ RCVDKVLNMS NSEIDKLDRY FFLYEMVKIT RNPQVLRDQC LNILLAGRDT
     TASLLSFAFF ELALNEPIWI KLRTEVLHVF QTSLELITFD LLKTKCPYLQ AILHETLRLY
     PSVPRNARFS KKNTTLPHGG GVDGMSPILI KKGQPVAYFI CATHVDEKFY TKDALIFRPE
     RWCEEPLIKK NLAWSYLPFN GGPRICLGQQ FALTEASYVL TRLAQCYTKI SLQPNSFEYP
     PKKQVHLTMS LLDGVHVKIS NLSIS