CY169_POSPM
ID CY169_POSPM Reviewed; 543 AA.
AC F1SYE5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Cytochrome P450 monooxygenase 169 {ECO:0000303|PubMed:21938516};
DE EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN Name=CYP169 {ECO:0000303|PubMed:21938516};
GN Synonyms=CYP5139D3v1 {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 7-
CC ethoxycoumarin, carbazole, phenanthrene and trans-stilbene as
CC substrates for oxidation. {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; AB573356; BAK09489.1; -; mRNA.
DR AlphaFoldDB; F1SYE5; -.
DR SMR; F1SYE5; -.
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 169"
FT /id="PRO_0000451354"
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; 60956 MW; 0ED4C0A64C25BD16 CRC64;
MTVTAVNVLL SLGVAALAVA VWKAVVMVIQ IATSPLRNIP GPPNSNWVYG NLKEIFAAEN
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 LRDELWSIPT
ENPSMDELNE LPYLEAVVRE TMRVHAPVPS TIRVAMTDDV IPLDTPFVDV HGQVQDSIRV
KKGDPIFIPI LVINRSKALW GEDAFEFKPE RWESVPDAVQ HIPGVWANQM SFLGGPRACI
GYRFSLIEMK ALIFALVRAF EFELAVPPEE IIKKSTAVQR PLVRSEMVKG CQLPLLIKPY
HTV