ID   CY205_POSPM             Reviewed;         543 AA.
AC   F1SYH0;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Cytochrome P450 monooxygenase 205 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP205 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5139D3v2 {ECO:0000303|PubMed:21938516};
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Dacryobolaceae; Postia.
OX   NCBI_TaxID=561896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=ATCC 44394 / Madison 698-R;
RX   PubMed=21938516; DOI=10.1007/s00203-011-0753-2;
RA   Ide M., Ichinose H., Wariishi H.;
RT   "Molecular identification and functional characterization of cytochrome
RT   P450 monooxygenases from the brown-rot basidiomycete Postia placenta.";
RL   Arch. Microbiol. 194:243-253(2012).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase that is able to use carbazole
CC       and phenanthrene as substrates for oxidation.
CC       {ECO:0000269|PubMed:21938516}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB573381; BAK09514.1; -; mRNA.
DR   AlphaFoldDB; F1SYH0; -.
DR   SMR; F1SYH0; -.
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:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..543
FT                   /note="Cytochrome P450 monooxygenase 205"
FT                   /id="PRO_0000451373"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         479
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|UniProtKB:P04798"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   543 AA;  61048 MW;  B30D5443ED31FEBD CRC64;
     MTVTAVNVLI SLGVAALAVA VWKAIVMVIQ IATSPLRNIP GPPNSNWVYG NLKEIFATEN
     SVLHEGWVAK YGNTIKYKGW LSRNRLFTVD TRALNYILSH SNEYQKPALA RYNLGEVLGE
     GLLIVEGEQH RQQRRIMNPA FGPAQIRELT EIFVEKAQKL CLFWRNEISK SGEPARIDVL
     NGLSKMTLDV IGLAGFNYEF DSLNIDGKPN ELNQAFSVMF RSLEGFAIVF PLLKALIPPL
     RLIPDGRSRR IAKARKVMRR MGMELITKKK AEILRAAAGE KEKDNLQSRD LLTLLIKANL
     ATDLPESHRL SDEDVLAQVP TFLVAGHETT SNATAWCLYA LTQAPEVQQK LREELWSIPT
     ENPSMDELNE LPYLEAVVRE TMRVHAPVPS TIRVAMTDDV IPLDTPFVDV HGQVQDSIRV
     KKGDPIFIPI LVINRSKALW GEDAFEFKPE RWESVPDAVQ HIPGVWANQM SFLGGPRACI
     GYRFSLIEMK ALIFALVRAF EFELAVPPEE IMKKSTAVQR PLVRSEMDKG CQLPLLIKPY
     HTV