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