ID   CP52X_CANMA             Reviewed;         526 AA.
AC   Q12581;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Cytochrome P450 52A5;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK2-A;
DE   AltName: Full=CYPLIIA5;
GN   Name=CYP52A5;
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=2039569; DOI=10.1089/dna.1991.10.271;
RA   Ohkuma M., Tanimoto T., Yano K., Takagi M.;
RT   "CYP52 (cytochrome P450alk) multigene family in Candida maltosa: molecular
RT   cloning and nucleotide sequence of the two tandemly arranged genes.";
RL   DNA Cell Biol. 10:271-282(1991).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=8713123; DOI=10.1006/bbrc.1996.1100;
RA   Zimmer T., Ohkuma M., Ohta A., Takagi M., Schunck W.H.;
RT   "The CYP52 multigene family of Candida maltosa encodes functionally diverse
RT   n-alkane-inducible cytochromes P450.";
RL   Biochem. Biophys. Res. Commun. 224:784-789(1996).
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 N-alkanes.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; X55881; CAA39366.1; -; Genomic_DNA.
DR   PIR; A40576; A40576.
DR   AlphaFoldDB; Q12581; -.
DR   SMR; Q12581; -.
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   1: Evidence at protein level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..526
FT                   /note="Cytochrome P450 52A5"
FT                   /id="PRO_0000423538"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         473
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   526 AA;  60261 MW;  5D56229D78111BB0 CRC64;
     MTSDSTIHEL IQSYITKWYV IVPLAIIIYK VFDYFYVLSL RKRLGAAVPT NEETDGYFGF
     HLPFVLMSKK KDGTIIDFSI ERYPELKHPE TPTFEFPIFT VKLISTIDPE NIKAILATQF
     SDFSLGTRHA HFAPLIGDGI FTLDGAGWKH SRAMLRPQFA REQVGHVKLL EPHVQVLFKH
     IRKNKGREFD LQELFFRFTV DSATEFLFGE SVESLRDASI GMTSKSKDVD GIEDFTGAFN
     YSQNYLASRS IMQQFYWILN GKKFRECNAI VHKFADHYVQ KALNLTEADL EKQAGYVFLY
     ELVKQTRDPQ VLRDQLLNIL VAGRDTTAGL LSFVFFELAR NPDVVAKLKD EIDTKFGLGE
     DARIEEITFE SLKQCEYLKA VLNECLRLYP SVPQNFRVAT KNTTLPRGGG KDGLSPILVR
     KGQTVMYSVY ATHRMESVYG KDATTFRPER WFEPETRKLG WAFVPFNGGP RICLGQQFAL
     TEASYVTVRL LQEFSTLTLD PNLEYPPKKM SHLTMSLFDG TNVQMY