ID   CP52H_CANTR             Reviewed;         517 AA.
AC   P30610;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cytochrome P450 52A8;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane-inducible P450-ALK5;
DE   AltName: Full=CYPLIIA8;
GN   Name=CYP52A8;
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. Preferentially hydroxylates
CC       lauric acid.
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; Z13012; CAA78356.1; -; Genomic_DNA.
DR   PIR; S22974; S22974.
DR   AlphaFoldDB; P30610; -.
DR   SMR; P30610; -.
DR   VEuPathDB; FungiDB:CTMYA2_002810; -.
DR   VEuPathDB; FungiDB:CTRG_03115; -.
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   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..517
FT                   /note="Cytochrome P450 52A8"
FT                   /id="PRO_0000052026"
FT   BINDING         464
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   517 AA;  59525 MW;  2C051CED38AD5839 CRC64;
     MYEQVVEYWY VVLPLVFILH KVFDMWHTRR LMKQLGAAPV TNQLHDNFFG IINGWKHLSS
     RKKVELKNIM IINLPIRKFQ VWVHMLVPSL EQSSSSQKIR RNIKALLATQ FSDFSLGKRH
     TLFKPLLGDG IFTLDGQGWK HSRAMLRPQF AREQVAHVTS LEPHFQLLKK HMVKNKGGFF
     DIQELFFRFT VDSATEFLFG ESVHSLKDET IGSYQDDIDF VGRKDFAESF NKAQEYLAIR
     TLVQDFYYLV NNQEFRDCNK LVHKFTNYYV QRALDATPEE LEKQSGYVFL YELVKQTRGP
     NVLRDQSLNI LLAGRDTSAG LLSFAVFELA RNPHIWAKLR EDVESQFGLG EQSRIEEITF
     ESLKRCGYLK AFLNETLRVY PSVPRNFRIA TKNTTLPRGG GSDGNSPVLV KKGEAVSYGI
     NSTHLDPVYY GDDAAEFRPE RWNEPSTRKL GWAYLPFNGG PRICLGQQFA LTEAGYVLVR
     LAQSFDTLEL KPPVVYPPKR LTNLTMSLQD GTIVKID