ID   CP52K_CANMA             Reviewed;         519 AA.
AC   Q12589;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Cytochrome P450 52A11;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK8;
DE   AltName: Full=CYPLIIA11;
GN   Name=CYP52A11;
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; BAA02214.1; -; Genomic_DNA.
DR   PIR; JS0726; JS0726.
DR   AlphaFoldDB; Q12589; -.
DR   SMR; Q12589; -.
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 52A11"
FT                   /id="PRO_0000052029"
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;  59476 MW;  70A9430ADEE38096 CRC64;
     MVFTAFILEY WYFTLLSLAA GHFIGKHVYT NYLMRKHHAE PILDVVDDGA FGFKFGFQAL
     KAKKIGKQID LLFKKFNEAK HPSIGTFVTR SFGMQFIATK DPENIKAMLA TQFNDFTLGQ
     RLSYFAPLLG KGIFTLDGEG WKHSRAMLRP QFSRDQVGHV KMLEPHFQLL KKHIIKNKGS
     FFDIQELFFR FTVDSATEFL FGESVSSLKD ESIGYDQEEI DFAGRKDFAE AFNKSQVYLS
     TRSLLQLLYW LVNSSDFKRC NKIVHKFSDY YIKKALTATP EELEKHSSYI FLYELAKQTR
     DPIVLRDQSL NILLAGRDTT AGLLSFAVFE LGRNPEVWSK LREEIGDKFG LDPDSRIEDI
     SFELLKLCEY LKAVINETLR LYPSVPRNGR FAAANTTLPH GGGPDGMSPI LVRKGQTVMY
     SVYALQRDEK YYGKDANEFR PERWFEPEVR KLGWAFLPFN GGPRICLGQQ FALTEASYVL
     VRLIQSFETL ELSPDAPYPP AKLTHLTMCL FDGAPVRIE