ID   CP52L_DEBHN             Reviewed;         519 AA.
AC   Q9Y757;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cytochrome P450 52A12;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane hydroxylase 1;
DE   AltName: Full=Alkane-inducible p450alk 1;
DE   AltName: Full=DH-ALK2;
GN   Name=CYP52A12; Synonyms=ALK1;
OS   Debaryomyces hansenii (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=4959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 20317;
RX   PubMed=9931473; DOI=10.1016/s0378-1119(98)00579-4;
RA   Yadav J.S., Loper J.C.;
RT   "Multiple p450alk (cytochrome P450 alkane hydroxylase) genes from the
RT   halotolerant yeast Debaryomyces hansenii.";
RL   Gene 226:139-146(1999).
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}.
CC   -!- INDUCTION: By N-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; AF103948; AAD22536.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y757; -.
DR   SMR; Q9Y757; -.
DR   VEuPathDB; FungiDB:DEHA2E18612g; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; Membrane; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..519
FT                   /note="Cytochrome P450 52A12"
FT                   /id="PRO_0000052030"
FT   BINDING         467
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   519 AA;  59167 MW;  AE44F34463FAD7DD CRC64;
     MFDVDTVHNF FTSWYGILLA VLIGYHVFDY IRIQIVMKKL GCVSPPVESD GFFGFKLLYT
     SLKHKKEGTL VNFIKERFET VGKDTFSFRI AGTPVISTKN PENIKALLAT QFSDFALGTR
     HAQFKPLLGD GIFTLDGSGW KHSRAMLRPQ FAREQVAHVK SLEPHIQMLA KHVRRAKGGA
     FDVQSLFFRL TVDSATEFLF GESVESLQDE SIGMAKDAVD FDGKAGFAEA FNTAQVYLSI
     RSLAQKAYFL VNNKEFRSSN EKVHKFADYY VQKALNSSPE ELEKHSQDGY IFLYELVKQT
     RDPHVLRDQL LNILLAGRDT TAGLLSFTFY ELARNPQVWS KLKEEIYEKF GKGDDARLED
     ITFESLKKCE YLKALLNEVL RLYPSVPQNF RVAQKDTSLP RGGGPNRDQP IFIAKGQTVT
     YTVYAMHRDE QFYGKDSEVF RPERWFEPET RKLGWAFLPF NGGPRICLGQ QFALTEASYV
     IARLAQLFPN LASHDDEYPP RKASHLTMCH QSEVKISLA