ABBA-type aromatic prenyltransferases (PTases); ABBA-type aromatic prenyltransferases (PTases) are a subgroup of prenyltransferases that are characterized by an unusual type of beta/alpha fold with antiparallel beta strands. They lack the (N/D)DxxD motif which is characteristic for many other prenyltransferases. Generally, aromatic prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto aromatic substrates, forming C-C bonds between C-1 or C-3 of the isoprenoid substrate and one of the aromatic carbons of the acceptor substrate by an electrophilic alkylation, or Friedel-Crafts alkylation mechanism.
The actual alignment was detected with superfamily member TIGR03430:
Pssm-ID: 473141 [Multi-domain] Cd Length: 419 Bit Score: 619.16 E-value: 0e+00
tryptophan dimethylallyltransferase; Members of this family are the enzyme tryptophan ...
1-315
0e+00
tryptophan dimethylallyltransferase; Members of this family are the enzyme tryptophan dimethylallyltransferase (EC 2.5.1.34), a distinct clade within a larger group of aromatic prenyltransferases that may act on on trp-containing cyclic dipeptides, or on tyrosine or other related substrates. Tryptophan dimethylallyltransferase and related enzymes typically are of fungal origin are involved in the biosynthesis of secondary metabolites such as ergot alkaloids.
Pssm-ID: 132471 [Multi-domain] Cd Length: 419 Bit Score: 619.16 E-value: 0e+00
Tryptophan dimethylallyltransferase; This family of proteins represents tryptophan ...
7-314
2.62e-128
Tryptophan dimethylallyltransferase; This family of proteins represents tryptophan dimethylallyltransferase (EC:2.5.1.34), which catalyzes the first step of ergot alkaloid biosynthesis. Ergot alkaloids, which are produced by endophyte fungi, can enhance plant host fitness, but also cause livestock toxicosis to host plants. This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 390 to 465 amino acids in length.
Pssm-ID: 463422 Cd Length: 356 Bit Score: 370.09 E-value: 2.62e-128
aromatic prenyltransferases (PTases) of the DMATS/CymD familiy; Members of the DMATS/CymD ...
10-314
6.64e-119
aromatic prenyltransferases (PTases) of the DMATS/CymD familiy; Members of the DMATS/CymD family of ABBA prenyltransferases prenylate indole, tyrosine, and xanthone derivatives. This family of fungal proteins includes cyclic dipeptide N-prenyltransferase (CdpNPT), Brevianamide F prenyltransferase (ftmPT1), fumigaclavine C synthase (FgaPT1), dimethylallyltryptophan synthase (DMATS) and related proteins. CdpNPT accepts a variety of tryptophan-containing cyclic dipeptides, including L-tryptophan itself, and prenylates these substrates inverse at the N-1 position of the indole group. FtmPT1 catalyzes the prenylation of brevianamide F in the biosynthesis of fumitremorgin-type alkaloids. FgaPT1 catalyses the prenylation of fumigaclavine A. Dimethylallyltryptophan synthases (DMATS) catalyzes the prenylation of L-tryptophan at C-4 of the indole ring during the biosynthesis of ergot alkaloids.
Pssm-ID: 260106 Cd Length: 392 Bit Score: 347.35 E-value: 6.64e-119
tryptophan dimethylallyltransferase; Members of this family are the enzyme tryptophan ...
1-315
0e+00
tryptophan dimethylallyltransferase; Members of this family are the enzyme tryptophan dimethylallyltransferase (EC 2.5.1.34), a distinct clade within a larger group of aromatic prenyltransferases that may act on on trp-containing cyclic dipeptides, or on tyrosine or other related substrates. Tryptophan dimethylallyltransferase and related enzymes typically are of fungal origin are involved in the biosynthesis of secondary metabolites such as ergot alkaloids.
Pssm-ID: 132471 [Multi-domain] Cd Length: 419 Bit Score: 619.16 E-value: 0e+00
aromatic prenyltransferase, DMATS type; Members of this protein family are mostly fungal ...
1-315
1.15e-133
aromatic prenyltransferase, DMATS type; Members of this protein family are mostly fungal enzymes of secondary metabolite production. Characterized or partially characterized members include several examples of dimethylallyltryptophan synthase, a brevianamide F prenyltransferase, LtxC from lyngbyatoxin biosynthesis, and a probable dimethylallyl tyrosine synthase.
Pssm-ID: 274575 Cd Length: 405 Bit Score: 385.51 E-value: 1.15e-133
Tryptophan dimethylallyltransferase; This family of proteins represents tryptophan ...
7-314
2.62e-128
Tryptophan dimethylallyltransferase; This family of proteins represents tryptophan dimethylallyltransferase (EC:2.5.1.34), which catalyzes the first step of ergot alkaloid biosynthesis. Ergot alkaloids, which are produced by endophyte fungi, can enhance plant host fitness, but also cause livestock toxicosis to host plants. This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 390 to 465 amino acids in length.
Pssm-ID: 463422 Cd Length: 356 Bit Score: 370.09 E-value: 2.62e-128
aromatic prenyltransferases (PTases) of the DMATS/CymD familiy; Members of the DMATS/CymD ...
10-314
6.64e-119
aromatic prenyltransferases (PTases) of the DMATS/CymD familiy; Members of the DMATS/CymD family of ABBA prenyltransferases prenylate indole, tyrosine, and xanthone derivatives. This family of fungal proteins includes cyclic dipeptide N-prenyltransferase (CdpNPT), Brevianamide F prenyltransferase (ftmPT1), fumigaclavine C synthase (FgaPT1), dimethylallyltryptophan synthase (DMATS) and related proteins. CdpNPT accepts a variety of tryptophan-containing cyclic dipeptides, including L-tryptophan itself, and prenylates these substrates inverse at the N-1 position of the indole group. FtmPT1 catalyzes the prenylation of brevianamide F in the biosynthesis of fumitremorgin-type alkaloids. FgaPT1 catalyses the prenylation of fumigaclavine A. Dimethylallyltryptophan synthases (DMATS) catalyzes the prenylation of L-tryptophan at C-4 of the indole ring during the biosynthesis of ergot alkaloids.
Pssm-ID: 260106 Cd Length: 392 Bit Score: 347.35 E-value: 6.64e-119
ABBA-type aromatic prenyltransferases (PTases); ABBA-type aromatic prenyltransferases (PTases) are a subgroup of prenyltransferases that are characterized by an unusual type of beta/alpha fold with antiparallel beta strands. They lack the (N/D)DxxD motif which is characteristic for many other prenyltransferases. Generally, aromatic prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto aromatic substrates, forming C-C bonds between C-1 or C-3 of the isoprenoid substrate and one of the aromatic carbons of the acceptor substrate by an electrophilic alkylation, or Friedel-Crafts alkylation mechanism.
Pssm-ID: 260105 Cd Length: 294 Bit Score: 136.47 E-value: 6.28e-38
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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