ID   CP52W_CANAP             Reviewed;         519 AA.
AC   Q12573;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cytochrome P450 52E2;
DE            EC=1.14.14.-;
DE   AltName: Full=CYPLIIE2;
GN   Name=CYP52E2;
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; X87640; CAA60980.1; -; Genomic_DNA.
DR   PIR; S69989; S69989.
DR   AlphaFoldDB; Q12573; -.
DR   SMR; Q12573; -.
DR   PRIDE; Q12573; -.
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 52E2"
FT                   /id="PRO_0000052037"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         461
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;  58631 MW;  F0B164E22D169C86 CRC64;
     MNINFSDALM LGGISLSFLL ASQAIYFYFI YSPRAKKLGC APPPIFFSFP LGIPDLIRLV
     NAWFHDDLLE WFTHRFEEFG RRTAFQSVAG QLWIGTIEPE NIKTMLATSF KDYSLGFRYN
     AMYGLLGNGI FTLSGDGWKN SRALLRPQFS REQVSHLESM RTHINMMINN HFKGGQVVDA
     QVLYHNLTID TATEFLFGES TNTLDPALAQ QGLPGPKGLV TGEQFAEAFT SALELLSVRV
     MAGAAWFLVW TPKFWRSCKV CHNFIDYFVY KALATPMEKG QDADRYVFIR ELTKETSDPR
     VIRDQALNIL LAGRDTTAAL LSFTTYYLGA YPEVYDELRE AVIADFGSAD AEPPTFEQLK
     QCKVLQNVIR EVLRLHPNVP LNFREAIADT TFPTGGGPNG DQPIFVPKGQ KVFYATYVMQ
     RNAGIWGPDS TSFRPDRWNE PREALASGWD YIPFNGGPRI CLGQQFALTE ASYTLVRICQ
     EFSRIEVLHP DVITARNVMK QRMRLPNSSS GGVITRFIR