ID   CY069_POSPM             Reviewed;         567 AA.
AC   F1SY70;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Cytochrome P450 monooxygenase 69 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP069 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5027B6v2 {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 4-
CC       ethoxybenzoic acid as a substrate 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}.
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; AB573281; BAK09414.1; -; mRNA.
DR   AlphaFoldDB; F1SY70; -.
DR   SMR; F1SY70; -.
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; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
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..567
FT                   /note="Cytochrome P450 monooxygenase 69"
FT                   /id="PRO_0000451359"
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         475
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        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   567 AA;  64002 MW;  2E4C4C857785E95C CRC64;
     MVISTNELAA LTVVLLATGV LFYANSTRRA PLPPGPRGLP LLGNLFQFDV MRPYPQYLKW
     AQKYGPVFSV KLGGQRIIVL NSSEAADELL ATRSKLYSSR ESPHVGFDLV SDQQRMLFMP
     YGREWKIARK NVHSLLGPGP SKQMGKTQDL ESRVMLHDLL CHGETSITEE FVEGPRGEVP
     ERHWFSIVRR YTTSVVMMLV YGRRIHRIVG NPELHKVYDL MSNFTHVSQP GRYMVDALPV
     LRWLPDMLAP WRAEGRKMHK REMDFWGKLF SDSRTAFLNG TGLNGFVQSY LRARTEAGLE
     DLPGNGATED AAGWMRDKLI TYTAVTIVEA GSDTTSTGVF SFVLLMLSNP DALQRAKEEM
     DAVVGSSRMP DWEDEDRLPW LTACIKETLR RAPPAPLGIP HKVDEDDVYN GYLIPKGSTV
     IGNIWAIHMD PVRYPDPTAF KPERFYNPDG KLNWASGPDA HNRDHYIFGW GRRFCSGKYL
     AEASMFIVLS RLIWGFDFYA ASDPQTGKAR LPDVSDVDTF TDGLVTAPKI YPVGFKPRSE
     KHAEMIKASY RDVQNDWQSM GLAGDER