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PENM_PENCR
ID   PENM_PENCR              Reviewed;         465 AA.
AC   A0A0E3D8L6;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=FAD-dependent monooxygenase penM {ECO:0000303|PubMed:26213965};
DE            EC=1.-.-.- {ECO:0000305|PubMed:26213965};
DE   AltName: Full=Penitrem biosynthesis cluster protein M {ECO:0000303|PubMed:26213965};
GN   Name=penM {ECO:0000303|PubMed:26213965};
OS   Penicillium crustosum (Blue mold fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC   STRAIN=PN2402;
RX   PubMed=26213965; DOI=10.3390/toxins7082701;
RA   Nicholson M.J., Eaton C.J., Starkel C., Tapper B.A., Cox M.P., Scott B.;
RT   "Molecular cloning and functional analysis of gene clusters for the
RT   biosynthesis of indole-diterpenes in Penicillium crustosum and P.
RT   janthinellum.";
RL   Toxins 7:2701-2722(2015).
CC   -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the indole diterpenes penitrems
CC       (PubMed:26213965). The geranylgeranyl diphosphate (GGPP) synthase penG
CC       catalyzes the first step in penitrem biosynthesis via conversion of
CC       farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl
CC       pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol
CC       phosphate with GGPP by the prenyl transferase penC then forms 3-
CC       geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-
CC       dependent monooxygenase penM leads to a epoxidized-GGI that is
CC       substrate of the terpene cyclase penB for cyclization to yield
CC       paspaline (Probable). Paspaline is subsequently converted to 13-
CC       desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter
CC       being then converted to paxilline by the cytochrome P450 monooxygenase
CC       penQ (PubMed:26213965). Paxilline is converted to beta-paxitriol via C-
CC       10 ketoreduction by the short-chain dehydrogenase PC-15 which can be
CC       monoprenylated at the C-20 by the indole diterpene prenyltransferase
CC       penD (Probable). A two-step elimination (acetylation and elimination)
CC       process performed by the O-acetyltransferase PC-16 and the
CC       P.simplicissimum ptmI-ortholog not yet identified in P.crustosum, leads
CC       to the production of the prenylated form of penijanthine (Probable).
CC       The FAD-linked oxidoreductase ptmO then converts the prenylated form of
CC       penijanthine into PC-M5 which is in turn transformed into PC-M4 by the
CC       aromatic dimethylallyltransferase PC-22 (Probable). A series of
CC       oxidation steps involving 4 cytochrome P450 monooxygenases (PC-21, PC-
CC       05, PC-23, PC-20) and a FAD-dependent monooxygenase (PC-14) are
CC       required for the transformation of PC-M4 to penitrems A and E.
CC       Synthesis of these final products is proposed to proceed via penitrems
CC       D and C (PC-21, PC-05, PC-14) and penitrems B and F (PC-21, PC-05, PC-
CC       14, PC-23) (Probable). {ECO:0000269|PubMed:26213965,
CC       ECO:0000305|PubMed:26213965}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:A6T923};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:26213965}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; KC963408; AGZ20191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3D8L6; -.
DR   SMR; A0A0E3D8L6; -.
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   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   3: Inferred from homology;
KW   FAD; Flavoprotein; Membrane; Monooxygenase; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..465
FT                   /note="FAD-dependent monooxygenase penM"
FT                   /id="PRO_0000446564"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        435..455
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         131
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         225..227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         299
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         309..313
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
SQ   SEQUENCE   465 AA;  52197 MW;  5419D9E4EAABB9C0 CRC64;
     MDKDQFHVII VGGSIAGLTL AHCLHRAGIS HVVLEKASEP APQIGASIGI LPNGARVLDQ
     LQLYETIEQY IEPLETATIG YPDGFRFSSS YPKLVNERFG FPIAFLDRQK LLEILYQHYP
     DKSRIRLAAR VVSIESSSID STITMEDGTI YKGHLIVGAD GVHSRVRAEM WKAAQRINPG
     MTVEYSCIFG ISAPIKGLIV GEQVNAFFDH LTIVTIHGKK GRVYWFLIQK LDRKYVYPEC
     PRFTAKEIGP IVNHLKEVKF FKDITFGQLW DSRETASMTA LEENVFDTWY HGRMVLMGDS
     AHKMTPNIGQ GANMAIEDAA VLSSLLSDLL QKQTQPPTNA QIEKLLAQYR EVRHPRVNSI
     YKTSRFLVRF QARDGIFNTL FGRYYAPHAG DLPADMASKT IAGGELCAYL PSPSRCSYGW
     EKYKNSGLGR TVWCVLVLLL SALTWSCLGN MNIIMELPKR VSMMR
 
 
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