CP52D_CANMA
ID CP52D_CANMA Reviewed; 538 AA.
AC P16141; Q12582;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 4.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cytochrome P450 52A4;
DE EC=1.14.14.-;
DE AltName: Full=Alkane-inducible P450-ALK3-A;
DE AltName: Full=CYPLIIA4;
DE AltName: Full=Cytochrome P450-CM2;
GN Name=CYP52A4;
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=2039569; DOI=10.1089/dna.1991.10.271;
RA Ohkuma M., Tanimoto T., Yano K., Takagi M.;
RT "CYP52 (cytochrome P450alk) multigene family in Candida maltosa: molecular
RT cloning and nucleotide sequence of the two tandemly arranged genes.";
RL DNA Cell Biol. 10:271-282(1991).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 2-15, AND FUNCTION.
RC STRAIN=EH15;
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 [4]
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.
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; X55881; CAA39367.1; -; Genomic_DNA.
DR EMBL; X51932; CAA36198.1; -; mRNA.
DR PIR; B40576; B40576.
DR PIR; S08668; O4CKA4.
DR AlphaFoldDB; P16141; -.
DR SMR; P16141; -.
DR PRIDE; P16141; -.
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"
FT CHAIN 2..538
FT /note="Cytochrome P450 52A4"
FT /id="PRO_0000052022"
FT TRANSMEM 27..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 485
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 2
FT /note="P -> S (in strain: EH15)"
FT VARIANT 39
FT /note="N -> P (in strain: EH15)"
FT VARIANT 235
FT /note="T -> V (in strain: EH15)"
FT VARIANT 299..300
FT /note="EA -> DD (in strain: EH15)"
FT VARIANT 442
FT /note="L -> S (in strain: EH15)"
FT VARIANT 449
FT /note="N -> S (in strain: EH15)"
FT VARIANT 514
FT /note="D -> N (in strain: EH15)"
FT VARIANT 527
FT /note="L -> V (in strain: EH15)"
SQ SEQUENCE 538 AA; 61911 MW; 82BAE8A329A62A4F CRC64;
MPVSFVHNVL EVVTPYVEYY QENLTKWYIL IPTILLTLNF LSILHTKYLE YKFNAKPLTN
FAQDYSFGVI TPLMLMYFKW HGTVMEFACN VWNNKFLVLN GNVRTVGLRI MGLNIIETTD
PENVKAILAT QFNDFSLGTR HDFLYSLLGD GIFTLDGAGW KHSRAMLRPQ FAREQVAHVK
LLEPHVQVLF KHVRKSQGKT FDIQELFFRL TVDSSTEFLF GGSVESLRDA SIGMTPSTKN
IAGREEFADA FNYSQTYNAY RFLLQQFYWI LNGSKFNKSI KTVHKFADFY VQKALSLTEA
DLEKQEGYVF LYELAKQTRD PKVLRDQLLN ILVAGRDTTA GLLSFLFFEL SRNPTVFEKL
KEEIHNRFGA KEDARVEEIT FESLKLCEYL KACVNEALRV YPSVPHNFRV ATRNTTLPRG
GGKDGMSPIA IKKGQNVMYT ILATHRDPNI YGEDANVFRP ERWFEPETRK LGWAYVPFNG
GPRICLGQQF ALTEASYVTV RLLQEFHTLT QDADTRYPPR LQNSLTLSLC DGANIQMY
