ID   CP52E_CANMA             Reviewed;         523 AA.
AC   P24458;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cytochrome P450 52A3-B;
DE            Short=CYP52A3-B;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK1-B;
DE   AltName: Full=CYPLIIA3;
GN   Name=CYP52A3-B;
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=1368716; DOI=10.1271/bbb1961.55.1757;
RA   Ohkuma M., Hikiji T., Tanimoto T., Schunck W.-H., Mueller H.G., Yano K.,
RA   Takagi M.;
RT   "Evidence that more than one gene encodes n-alkane-inducible cytochrome P-
RT   450s in Candida maltosa, found by two-step gene disruption.";
RL   Agric. Biol. Chem. 55:1757-1764(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-13, AND INDUCTION.
RC   STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977;
RX   DOI=10.1271/bbb1961.53.2217;
RA   Takagi M., Ohkuma M., Kobayashi N., Watanabe M., Yano K.;
RT   "Purification of cytochrome P-450alk from n-alkane-grown cells of Candida
RT   maltosa, and cloning and nucleotide sequencing of the encoding gene.";
RL   Agric. Biol. Chem. 53:2217-2226(1989).
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; Single-pass
CC       membrane protein.
CC   -!- INDUCTION: By alkanes. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D12475; BAA02041.1; -; Genomic_DNA.
DR   EMBL; S77461; AAC60531.1; -; Genomic_DNA.
DR   PIR; JQ1039; JQ1039.
DR   AlphaFoldDB; P24458; -.
DR   SMR; P24458; -.
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   Direct protein sequencing; Heme; Iron; Membrane; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..523
FT                   /note="Cytochrome P450 52A3-B"
FT                   /id="PRO_0000052023"
FT   TRANSMEM        17..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         471
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   523 AA;  59869 MW;  DB357103097F7FE8 CRC64;
     MAIEQIIEEV LPYLTKWYTI LFGAAFTYFL SIALRNKYYE YKLKCENPPY FKTAGFVGIP
     GLIDVIKAKN AGKLADYADQ TFDEYPHHSF YMTVAGMLKI VLTVDPENIK AVLATQFNDF
     ALGARHAHFD PLLGDGIFTL DGEGWKHSRA MLRPQFAREQ IAHVKALEPH VQVLAKQIKL
     NKGETFDLQE LFFRFTVDTA TEFLFGESVH SLYDEKLGVP PPNNIPGREN FAKAFNTSQH
     YLATRTYSQM FYFLTNPKEF RDCNAKVHKL AQYFVNKALD ASEDEVAEKS KGGYVFLYEL
     VKQTRDPKVL QDQLLNIMVA GRDTTAGLLS FAMFELARNP KIWNKLREEI EVNFGLGEEA
     RVDEISFETL KKCEYLKAVL NETLRMYPSV PVNFRTATRD TTLPRGGGKD GTSPIFVPKG
     SSVVYTVYKT HRLEEYYGKD AYEFRPERWF EPSTRKLGWA YVPFNGGPRI CLGQQFALTE
     ASYVITRLAQ MFEHLESKDE TYPPNKCIHL TMNHNEGVFI SAK