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CY074_POSPM
ID   CY074_POSPM             Reviewed;         508 AA.
AC   F1SY73;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Cytochrome P450 monooxygenase 74 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP074 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5158B2 {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 3,5-
CC       dimethoxy-trans-stilbene and 3,5,4'-trimethoxy-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; AB573284; BAK09417.1; -; mRNA.
DR   AlphaFoldDB; F1SY73; -.
DR   SMR; F1SY73; -.
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; IPR017972; Cyt_P450_CS.
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.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..508
FT                   /note="Cytochrome P450 monooxygenase 74"
FT                   /id="PRO_0000451400"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         438
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        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   508 AA;  56646 MW;  E3E901F996BCDEAD CRC64;
     MRDSLARNIL LPTAPSLGAI ACLLLAIAIG LLLLPRSQPH CFPPGPPVKP IVGSILQVSP
     QGAWYKFSEY QKVYGDLLFF RGLGSHVLVL NSMKAINDLL DKRSSVYSNR PTFTVVGELM
     GLGQSMPLLP YGEEWRAHRR LAHSALSPTA VRRYHGIQED MAALLCMRLL REPEAFFSHV
     RLIAGNIILS VVYGLPVETS EDEYIAHAER TMQVIGKATV PGAYLCDLMP FLKHLPSWVP
     FQREASTGRE MIERLVTKPF EHVKRAMEAG SAPPSVTQDL LSTNIDDMHD VEQRIKWTTG
     AMYGAGGETT YSTVLVFIMA MALHPEKQQR AQQEIDRVIG IERFPRISDR AHLPYVNAVI
     KETMRWHPVL PLSIARMSAQ DDLYDGYSIP EGTVVIPNIW GIANDCPRAT EFDPERFLNE
     GAPVDPSSWA FGFGKRLCPG KFLGENSVFI LITALLAIFD ITPNSSEDLQ PDFTLDLVSY
     PRPFKCRIQP RSEGHAQLAI SRAAQRSF
 
 
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