ID   CP52I_CANMA             Reviewed;         521 AA.
AC   Q12586;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cytochrome P450 52A9;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK5-A;
DE   AltName: Full=CYPLIIA9;
GN   Name=CYP52A9;
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).
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; D12717; BAA02211.1; -; Genomic_DNA.
DR   PIR; JS0723; JS0723.
DR   AlphaFoldDB; Q12586; -.
DR   SMR; Q12586; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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.
FT   CHAIN           1..521
FT                   /note="Cytochrome P450 52A9"
FT                   /id="PRO_0000052027"
FT   BINDING         468
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   521 AA;  59872 MW;  07D8827DC92042DA CRC64;
     MIDEILPKLV QYWYIVLPTL LIIKHVVSYI NTQRLMRKFR AKPVTNVLND GFFGIPNGIK
     AIKEKNKGRA QEYNDEKFAA GPKPKVGTYL FKLFTKDVLV TKDPENIKAI LATQFEDFSL
     GKRLDFFKPL LGYGIFTLDG EGWKHSRAML RPQFAREQVG HVKLIEPHFQ SLKKHIIKNK
     GQFFDIQELF FRFTVDSATE FLFGESVESL KDESIGYDQQ DFDFDGRKNF AEAFNKAQEY
     LGTRAILQLF YWLVNGADFK KSVAEVHKFT DYYVQKALDA TPEELEKHSG YIFLYELVQQ
     TRDPKVLRDQ SLNILLAGRD TTAGLLSFAL FELARNPEVW SRLREEIGDK FGLDEDATIE
     GISFESLKQC EYLKAVVNEC LRMYPSVPRN FRIATKHTTL PRGGGPDGKD PIFIKKGAVV
     SYGINSTHLD PMYYGPDARL FNPDRWSKPE TKKLGWAFLP FNGGPRICLG QQFALTEASY
     VLVRMIQNFK ELELTPNTVY PPRRLTNLTM SLYDGAYIKV N