ID   CP52J_CANMA             Reviewed;         519 AA.
AC   Q12588;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cytochrome P450 52A10;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK7;
DE   AltName: Full=CYPLIIA10;
GN   Name=CYP52A10;
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}.
CC   -!- INDUCTION: By N-alkanes.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D12719; BAA02213.1; -; Genomic_DNA.
DR   PIR; JS0725; JS0725.
DR   AlphaFoldDB; Q12588; -.
DR   SMR; Q12588; -.
DR   PRIDE; Q12588; -.
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   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..519
FT                   /note="Cytochrome P450 52A10"
FT                   /id="PRO_0000052028"
FT   BINDING         466
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   519 AA;  59750 MW;  A971D5604E11230A CRC64;
     MIFTAFILDY WYFTLLFLIA AYFIGKHVYT NYLMRKHHAE PILDVVDDGA FGFKFGFQSL
     KAKKIGNQID LLFLKFNEAK HPSIGTFVTR SFGMQFIATK DPENIKAMLA TQFNEYTLGQ
     RLNFLAPLLG KGIFTLDGNG WKHSRAMLRP QFSRDQIGHV KMLEPHFQLL KKHIIKNKGT
     FFDIQELFFR FTVDSATEFL FGESVSSLKD ESIGYDQEEI DFAGRKDFAE AFNKSQVYLS
     TRTLLQLLYW LVNSADFKRC NKIVHKFSDY YIKKALTATP EELEKHSSYI FLYELAKQTR
     DPIVLRDQSL NILLAGRDTT AGLLSFAVFE LGRNPEVWSK LRQEIGHKFG LDSYSRVEDI
     SFELLKLCEY LKAVLNETLR LYPSVPRNAR FAAKNTTLPH GGGPDGMSPI LVRKGQTVMY
     SVYALQRDEK YYGKDANEFR PERWFEPEVR KLGWAFLPFN GGPRICLGQQ FALTEASYVL
     ARLIQSFETL ELSPEAAYPP AKLSHLTMCL FDGTPVRFE