ID   CP52N_CANTR             Reviewed;         506 AA.
AC   P30611;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Cytochrome P450 52B1;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK6;
DE   AltName: Full=CYPLIIB1;
GN   Name=CYP52B1;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX   PubMed=1457045; DOI=10.1089/dna.1992.11.767;
RA   Seghezzi W., Meili C., Ruffiner R., Kuenzi R., Sanglard D., Fiechter A.;
RT   "Identification and characterization of additional members of the
RT   cytochrome P450 multigene family CYP52 of Candida tropicalis.";
RL   DNA Cell Biol. 11:767-780(1992).
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   -!- INDUCTION: By various 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; Z13013; CAA78357.1; -; Genomic_DNA.
DR   PIR; S22975; S22975.
DR   AlphaFoldDB; P30611; -.
DR   SMR; P30611; -.
DR   VEuPathDB; FungiDB:CTMYA2_002800; -.
DR   VEuPathDB; FungiDB:CTRG_03114; -.
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; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR01239; EP450IICYP52.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..506
FT                   /note="Cytochrome P450 52B1"
FT                   /id="PRO_0000052032"
FT   BINDING         451
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   506 AA;  58541 MW;  90122E03614E3B69 CRC64;
     MSLTETTATF IYNYWYIIFH LYFYTTSKII KYHHTTYLMI KFKASPPLNY INKGFFGIQA
     TFTELKHLIC HTSIDYAIDQ FNNVPFPHVH TFVTKVLGNE LIMTKDPENI KVLLRFPVFD
     KFDYGTRSSA VQPSLGMGIF TLEGENWKAT RSVLRNMFDR KSIDKVHDFE PHFKTLQKRI
     DGKVGYFDIQ QEFLKLGLEL SIEFIFGQVV SEDVPHYDDF TQAWDRCQDY MMLRLLLGDF
     YWMANDWRYK QSNQIVQAFC DYLVQKSLEN TCNDKFVFVH QLAKHTTNKT FIRDQALSLI
     MASRDTTAEL MAFTILELSR KSHHLGKLRE EIDANFGLES PDLLTFDSLR KFKYVQAILN
     ETLRMYPGVP RNMKTAKCTT TLPKGGGPDG QDPILVKKGQ SVGFISIATH LDPVLNFGSD
     AHVFRPDRWF DSSMKNLGCK YLPFNAGPRT CLGQQYTLIE ASYLLVRLAQ TYETVESHPD
     SVYPPRKKAL INMCAADGVD VKFHRL