ID   CP52V_CANAP             Reviewed;         519 AA.
AC   P43083;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cytochrome P450 52E1;
DE            EC=1.14.14.-;
DE   AltName: Full=CYPLIIE1;
GN   Name=CYP52E1;
OS   Candida apicola (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Starmerella.
OX   NCBI_TaxID=29830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IMET 43747;
RX   PubMed=8771711;
RX   DOI=10.1002/(sici)1097-0061(199605)12:6<565::aid-yea951>3.0.co;2-6;
RA   Lottermoser K., Schunck W.H., Asperger O.;
RT   "Cytochromes P450 of the sophorose lipid-producing yeast Candida apicola:
RT   heterogeneity and polymerase chain reaction-mediated cloning of two
RT   genes.";
RL   Yeast 12:565-575(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}. Membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; X76225; CAA53811.1; -; Genomic_DNA.
DR   PIR; S69988; S69988.
DR   AlphaFoldDB; P43083; -.
DR   SMR; P43083; -.
DR   PRIDE; P43083; -.
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   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..519
FT                   /note="Cytochrome P450 52E1"
FT                   /id="PRO_0000052036"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         479
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;  58656 MW;  4185235A07EA4370 CRC64;
     MIIGLSDAFA LGGIALSFLV AYQFIYFYFI YSPRAKKLGC APPVIVFSFP LGLPALYKFA
     TAMLHDNLLE YISIRIADMK VRTGFQTLAG QRWLVTLEPE NIKTVLATSF KDYSLGFRYD
     IMYGLLGNGI FTLSGDGWKH SRALLRPQFS REQVSHLESM RTHINLMINN HFKGGQVVDA
     QALYHNLTID TATEFLFGES TNTLDPDLAQ QGLPGPKGLV TGEQFAEAFT SALEILSVRV
     IVGAAWFLIW TPKFWRSCKV CHNFIDYFVY KALATPMEKD QEADRYVFIR ELTKETSDPR
     VIRDQALNIL LAGRDTTAGL LSFITYYLGA YPEVYAELRE AVLSEFGSTD VETPTFEQLK
     QCKVLQNVIR EVLRLHPNVP LNFRQAIVDT KLPTGGGPNG DQPVFVPKGQ NVFYSTYSMQ
     RRTDIWGPDA TTFRPDRWNE PREALASGWD YIPFNGGPRI CLGQQFALTE ASYTIVRICQ
     EFSRIEVLHP DVITSKNSMK QRMRLTQTAS GGVITRFIR