CP52C_CANMA
ID CP52C_CANMA Reviewed; 523 AA.
AC P16496; O94080; P20017;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cytochrome P450 52A3-A;
DE Short=CYP52A3-A;
DE EC=1.14.14.-;
DE AltName: Full=Alkane-inducible P450-ALK1-A;
DE AltName: Full=CYPLIIA3;
DE AltName: Full=Cytochrome P-450ALK;
DE AltName: Full=Cytochrome P450-CM1;
GN Name=CYP52A3-A;
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], 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=EH15;
RX PubMed=2735924; DOI=10.1016/0006-291x(89)92677-6;
RA Schunck W.-H., Kaergel E., Gross B., Wiedmann B., Mauersberger S.,
RA Koepke K., Kiessling U., Strauss M., Gaestel M., Mueller H.-G.;
RT "Molecular cloning and characterization of the primary structure of the
RT alkane hydroxylating cytochrome P-450 from the yeast Candida maltosa.";
RL Biochem. Biophys. Res. Commun. 161:843-850(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=EH15;
RX PubMed=1935996;
RA Schunck W.-H., Vogel F., Gross B., Kaergel E., Mauersberger S., Koepke K.,
RA Gengnagel C., Mueller H.-G.;
RT "Comparison of two cytochromes P-450 from Candida maltosa: primary
RT structures, substrate specificities and effects of their expression in
RT Saccharomyces cerevisiae on the proliferation of the endoplasmic
RT reticulum.";
RL Eur. J. Cell Biol. 55:336-345(1991).
RN [4]
RP PROTEIN SEQUENCE OF 2-16, AND FUNCTION.
RX PubMed=8645001; DOI=10.1006/abbi.1996.0170;
RA Scheller U., Zimmer T., Kargel E., Schunck W.H.;
RT "Characterization of the n-alkane and fatty acid hydroxylating cytochrome
RT P450 forms 52A3 and 52A4.";
RL Arch. Biochem. Biophys. 328:245-254(1996).
RN [5]
RP CHARACTERIZATION.
RX PubMed=8713123; DOI=10.1006/bbrc.1996.1100;
RA Zimmer T., Ohkuma M., Ohta A., Takagi M., Schunck W.H.;
RT "The CYP52 multigene family of Candida maltosa encodes functionally diverse
RT n-alkane-inducible cytochromes P450.";
RL Biochem. Biophys. Res. Commun. 224:784-789(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. {ECO:0000269|PubMed:8645001}.
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.1}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D00481; BAA00371.1; -; Genomic_DNA.
DR EMBL; M27081; AAA34320.1; -; mRNA.
DR EMBL; X51931; CAA36197.1; -; mRNA.
DR PIR; B56578; O4CKA3.
DR AlphaFoldDB; P16496; -.
DR SMR; P16496; -.
DR PRIDE; P16496; -.
DR BioCyc; MetaCyc:MON-18777; -.
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|PubMed:8645001, ECO:0000269|Ref.1"
FT CHAIN 2..523
FT /note="Cytochrome P450 52A3-A"
FT /id="PRO_0000052021"
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"
FT VARIANT 21
FT /note="L -> I (in strain: EH15)"
FT VARIANT 52
FT /note="E -> Q (in strain: EH15)"
FT VARIANT 147
FT /note="L -> H (in strain: EH15)"
FT CONFLICT 217
FT /note="L -> S (in Ref. 2; AAA34320)"
FT /evidence="ECO:0000305"
FT CONFLICT 220..221
FT /note="Missing (in Ref. 2; AAA34320)"
FT /evidence="ECO:0000305"
FT CONFLICT 231..232
FT /note="FA -> VR (in Ref. 2; AAA34320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 59840 MW; 5E5B7EE432DEE30F CRC64;
MAIEQIIEEV LPYLTKWYTI LFGAAVTYFL SIALRNKFYE YKLKCENPVY FEDAGLFGIP
ALIDIIKVRK AGQLADYTDT TFDKYPNLSS YMTVAGVLKI VFTVDPENIK AVLATQFNDF
ALGARHAHFD PLLGDGIFTL DGEGWKLSRA MLRPQFAREQ IAHVKALEPH VQILAKQIKL
NKGKTFDLQE LFFRFTVDTA TEFLFGESVH SLYDEKLGIP APNDIPGREN FAEAFNTSQH
YLATRTYSQI FYWLTNPKEF RDCNAKVHKL AQYFVNTALN ATEKEVEEKS KGGYVFLYEL
VKQTRDPKVL QDQLLNIMVA GRDTTAGLLS FAMFELARNP KIWNKLREEV EVNFGLGDEA
RVDEISFETL KKCEYLKAVL NETLRMYPSV PINFRTATRD TTLPRGGGKD GNSPIFVPKG
SSVVYSVYKT HRLKQFYGED AYEFRPERWF EPSTRKLGWA YLPFNGGPRI CLGQQFALTE
ASYVIARLAQ MFEHLESKDE TYPPNKCIHL TMNHNEGVFI SAK
