ID   CP52B_CANTR             Reviewed;         522 AA.
AC   P30607;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cytochrome P450 52A2;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK2;
DE   AltName: Full=CYPLIIA2;
GN   Name=CYP52A2;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX   PubMed=1937041; DOI=10.1016/0378-1119(91)90565-s;
RA   Seghezzi W., Sanglard D., Fiechter A.;
RT   "Characterization of a second alkane-inducible cytochrome P450-encoding
RT   gene, CYP52A2, from Candida tropicalis.";
RL   Gene 106:51-60(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 312-522.
RC   STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX   PubMed=2806542; DOI=10.1016/0014-5793(89)81732-6;
RA   Sanglard D., Fiechter A.;
RT   "Heterogeneity within the alkane-inducible cytochrome P450 gene family of
RT   the yeast Candida tropicalis.";
RL   FEBS Lett. 256:128-134(1989).
RN   [3]
RP   TOPOLOGY.
RX   PubMed=8375386; DOI=10.1111/j.1432-1033.1993.tb18166.x;
RA   Sanglard D., Sengstag C., Seghezzi W.;
RT   "Probing the membrane topology of Candida tropicalis cytochrome P450.";
RL   Eur. J. Biochem. 216:477-485(1993).
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. Preferentially hydroxylates
CC       hexadecane.
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 various alkanes.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M63258; AAA34353.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; X17560; CAA35593.1; ALT_SEQ; Genomic_DNA.
DR   PIR; JT0980; JT0980.
DR   AlphaFoldDB; P30607; -.
DR   SMR; P30607; -.
DR   VEuPathDB; FungiDB:CTMYA2_042620; -.
DR   VEuPathDB; FungiDB:CTRG_01061; -.
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..522
FT                   /note="Cytochrome P450 52A2"
FT                   /id="PRO_0000052020"
FT   TRANSMEM        14..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         469
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   522 AA;  60151 MW;  9ED1D8FF33040A50 CRC64;
     MSIQDIVETY STKWYVVVLV ALIVYKVFDF FYARYLMYKL GAKPFLQSQT DGYLGFRVPF
     ELMGKKSEGT LIDFTYQRTL ELDNPDIPTF TFPIFSVLII STLEPDNIKA ILATQFNDFS
     LGTRHSHFAP LLGDGIFTLD GAGWKHSRSM LRPQFAREQV SHVKLLEPHM QVFFKHIRKH
     HGQTFDIQEL FFRLTVDSAT EFLFGESVES LRDESIGMLN DALDFDGKAG FADAFNYSQN
     YLASRALMQQ MYWILNGKKF KECNAKVHKF ADYYVEKALE LTPDQLEKQD GYVFLYELVK
     QTRDRQVLRD QLLNILVAGR DTTAGLLSFV FFELARTPRV ANKLREEIED KFGLGQDARV
     EEISFESLKS CEYLKAVLNE CLRLYPSVPQ NFRVATRNTT LPRGGGKDGL SPVLVRKGQT
     VMYSVYAAHR NKQIYGEDAL EFRPERWFEP ETKKLGWAFL PFNGGPRICL GQQFALTEAS
     YVTVRLLQEF SHLTMDPNTE YSPKKMSHLT MSLFDGANIQ MY