ID   CP52A_CANTR             Reviewed;         543 AA.
AC   P10615;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Cytochrome P450 52A1;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK1;
DE   AltName: Full=CYPLIIA1;
GN   Name=CYP52A1;
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=2663647; DOI=10.1016/0378-1119(89)90014-0;
RA   Sanglard D., Loper J.C.;
RT   "Characterization of the alkane-inducible cytochrome P450 (P450alk) gene
RT   from the yeast Candida tropicalis: identification of a new P450 gene
RT   family.";
RL   Gene 76:121-136(1989).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 438-543.
RC   STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX   PubMed=3579905; DOI=10.1016/s0006-291x(87)80503-x;
RA   Sanglard D., Chen C., Loper J.C.;
RT   "Isolation of the alkane inducible cytochrome P450 (P450alk) gene from the
RT   yeast Candida tropicalis.";
RL   Biochem. Biophys. Res. Commun. 144:251-257(1987).
RN   [4]
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.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum 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; M24894; AAA63568.1; -; Genomic_DNA.
DR   EMBL; M63258; AAA34354.1; -; Genomic_DNA.
DR   EMBL; M15945; AAA34334.1; -; Genomic_DNA.
DR   PIR; JS0203; JS0203.
DR   AlphaFoldDB; P10615; -.
DR   SMR; P10615; -.
DR   VEuPathDB; FungiDB:CTMYA2_042610; -.
DR   VEuPathDB; FungiDB:CTRG_01060; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..543
FT                   /note="Cytochrome P450 52A1"
FT                   /id="PRO_0000052019"
FT   TOPO_DOM        1..28
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:8375386"
FT   TRANSMEM        29..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        49..543
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:8375386"
FT   BINDING         487
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"
FT   CONFLICT        70
FT                   /note="C -> G (in Ref. 2; AAA34354)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   543 AA;  62499 MW;  78CE3C4865EE1288 CRC64;
     MSSSPSIAQE FLATITPYVE YCQENYTKWY YFIPLVILSL NLISMLHTKY LERKFKAKPL
     AVYVQDYTFC LITPLVLIYY KSKGTVMQFA CDLWDKNLIV SDPKAKTIGL KILGIPLIET
     KDPENVKAIL ATQFNDFSLG TRHDFLYSLL GDGIFTLDGA GWKHSRTMLR PQFAREQVSH
     VKLLEPHMQV LFKHIRKHHG QTFDIQELFF RLTVDSATEF LLGESAESLR DESVGLTPTT
     KDFDGRNEFA DAFNYSQTNQ AYRFLLQQMY WILNGSEFRK SIAIVHKFAD HYVQKALELT
     DEDLEKKEGY VFLFELAKQT RDPKVLRDQL LNILVAGRDT TAGLLSFLFF ELSRNPEIFA
     KLREEIENKF GLGQDARVEE ISFETLKSCE YLKAVINETL RIYPSVPHNF RVATRNTTLP
     RGGGEGGLSP IAIKKGQVVM YTILATHRDK DIYGEDAYVF RPERWFEPET RKLGWAYVPF
     NGGPRICLGQ QFALTEASYV TVRLLQEFGN LKQDPNTEYP PKLQNTLTLS LFEGAEVQMY
     LIL