ID   CP52M_DEBHN             Reviewed;         519 AA.
AC   Q9Y758;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Cytochrome P450 52A13;
DE            EC=1.14.14.-;
DE   AltName: Full=Alkane hydroxylase 2;
DE   AltName: Full=Alkane-inducible p450alk 2;
DE   AltName: Full=DH-ALK2;
GN   Name=CYP52A13; Synonyms=ALK2;
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}.
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DR   EMBL; AF103949; AAD22537.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y758; -.
DR   SMR; Q9Y758; -.
DR   VEuPathDB; FungiDB:DEHA2C02596g; -.
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 52A13"
FT                   /id="PRO_0000052031"
FT   BINDING         466
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;  59607 MW;  1CE7D1EE29CE5E5A CRC64;
     MSELLDSIQP YLTKWYVVIS ALLVSFFIAH KISVARFKAT HNCAASPEYY KVNWFSLPLL
     YRLIQVKREG RLLDFAQKIY DDVKALTFVI KIVGVPVIIT RDPENMKAVL ATQFNDFALG
     TRHAHFKPLL GDGIFTLDGN GWKQSRSMLR PQFSREQVAH VQALEPHLQR LAKHIRLADG
     ETINIQDLFF KLTVDTATEF LFGQSVYSLK DAAINDPPTE DFDGRSSFAN SFNTAQTYLG
     TRAYLQMFYF IVNNSDFRKC CKQVHDFTRF YVQKGLDMTP EELEKKSENG YVFLYELVKQ
     TRDPKVLQDQ LLNILLAGRD TTAGLLSFTF FELARHPRVF NKLKEEIYEA FGKGDDARVS
     EITFESLKKC EYLKWVMNEM LRLYPSVPVN FRVATKRTTL PRGGGPDGNS PIYVGKGTTV
     AYSVYSTHRM EEYYGKDADE FKPERWAESR KLGWAYVPFN GGPRICLGQQ FALTEASYIV
     TRLLQMFDKL ELHDDRPYPP AKSVHLTMCH QDGVYVSLS