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DPASE_ARTSH
ID   DPASE_ARTSH             Reviewed;         476 AA.
AC   P9WEX4;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   03-AUG-2022, entry version 6.
DE   RecName: Full=FAD-dependent monooxygenase dpasE {ECO:0000303|PubMed:32286350};
DE            EC=1.-.-.- {ECO:0000269|PubMed:32286350};
DE   AltName: Full=Diterpenoid pyrone biosynthesis cluster protein E {ECO:0000303|PubMed:32286350};
DE   Flags: Precursor;
GN   Name=dpasE {ECO:0000303|PubMed:32286350};
OS   Arthrinium sacchari (Coniosporium sacchari).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Apiosporaceae; Apiospora.
OX   NCBI_TaxID=166626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   AND BIOTECHNOLOGY.
RX   PubMed=32286350; DOI=10.1038/s41467-020-15664-4;
RA   Tsukada K., Shinki S., Kaneko A., Murakami K., Irie K., Murai M.,
RA   Miyoshi H., Dan S., Kawaji K., Hayashi H., Kodama E.N., Hori A., Salim E.,
RA   Kuraishi T., Hirata N., Kanda Y., Asai T.;
RT   "Synthetic biology based construction of biological activity-related
RT   library of fungal decalin-containing diterpenoid pyrones.";
RL   Nat. Commun. 11:1830-1830(2020).
CC   -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the diterpenoid pyrones subglutinols A and
CC       B (PubMed:32286350). The first step of the pathway is the synthesis of
CC       the alpha-pyrone moiety by the polyketide synthase dpasA via
CC       condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units
CC       and 2 methylations (PubMed:32286350). The alpha-pyrone is then combined
CC       with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase
CC       dpasD through the action of the prenyltransferase dpasC to yield a
CC       linear alpha-pyrone diterpenoid (PubMed:32286350). Subsequent steps in
CC       the diterpenoid pyrone biosynthetic pathway involve the decalin core
CC       formation, which is initiated by the epoxidation of the C10-C11 olefin
CC       by the FAD-dependent oxidoreductase dpasE, and is followed by a
CC       cyclization cascade catalyzed by the terpene cyclase dpasB
CC       (PubMed:32286350). The FAD-linked oxidoreductase dpasF is then involved
CC       in tetrahydrofuran (THF) ring formation at the C5 unit to complete the
CC       formation of subglutinols A and B (PubMed:32286350). DpasF possesses
CC       also an additional catalytic ability of multi-step oxidations to
CC       generate a new DDP analog with an enone system at the C5 named FDDP A
CC       (PubMed:32286350). {ECO:0000269|PubMed:32286350}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:32286350}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- BIOTECHNOLOGY: Diterpenoid pyrones display various biological
CC       activities and subglutinol A shows insecticidal and anti-HIV
CC       activities. {ECO:0000269|PubMed:32286350}.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P9WEX4; -.
DR   SMR; P9WEX4; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..476
FT                   /note="FAD-dependent monooxygenase dpasE"
FT                   /id="PRO_0000451542"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         35..36
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         132
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         233..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         308
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         318..322
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   476 AA;  53436 MW;  D9E8FD2BFD3E450D CRC64;
     MSQPAFKIII VGCSVTGLTL AHCLDKLGVE YTILEKRSAV VLQEGASVAV MPNGGRILDQ
     LGLYDAFEKA TVPLDLTDAY LPDQDFRFTS DYPRRVLATF GYPVAFMERR GLLEILYDGI
     ADKSKIHLNK GVTHVEQNDD GAKVHTEDGE VYEGDIVVGA DGIHSKTLRE MWRMMGEPVV
     NGIAQSESQN MSVAFSCVFG ISHDVPELQP GEQILRMCNG STIFVMGSKG VVFWFIVTQL
     NRRYEYHDAP RYTTEEAAAF CEARKDAEIK EGVTFECIWR KQHVFNMLPL QESLFQTWSH
     GRVVCIGDSV HKMTINLGQG ANCAIEDVTV LCNMLRAFLA EKREKKPSYS EIDTLLRRFN
     KEHLPRASTI VETSRLTTRV HAQVGISQRI MTRWVVPYFG KFLQGKPLGL IASGPVLDFL
     PLKRASYPGW ERYRVKKSSR GAGFWITAFL SLSLLAVAAT MYGWGNSQIW ADWNIL
 
 
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