tryptophanase is a bacterial pyridoxal 5'-phosphate (PLP)-dependent lyase that catalyses in vivo degradation of l-tryptophan to yield indole, pyruvate and ammonia
tryptophanase, leader peptide-associated; Members of this family belong to the ...
5-471
0e+00
tryptophanase, leader peptide-associated; Members of this family belong to the beta-eliminating lyase family (pfam01212) and act as tryptophanase (L-tryptophan indole-lyase). The tryptophanases of this family, as a rule, are found with a tryptophanase leader peptide (TnaC) encoded upstream. Both tryptophanases (4.1.99.1) and tyrosine phenol-lyases (EC 4.1.99.2) are found between trusted and noise cutoffs, but this model captures nearly all tryptophanases for which the leader peptide gene tnaC can be found upstream. [Energy metabolism, Amino acids and amines]
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Pssm-ID: 131666 Cd Length: 467 Bit Score: 994.83 E-value: 0e+00
tryptophanase, leader peptide-associated; Members of this family belong to the ...
5-471
0e+00
tryptophanase, leader peptide-associated; Members of this family belong to the beta-eliminating lyase family (pfam01212) and act as tryptophanase (L-tryptophan indole-lyase). The tryptophanases of this family, as a rule, are found with a tryptophanase leader peptide (TnaC) encoded upstream. Both tryptophanases (4.1.99.1) and tyrosine phenol-lyases (EC 4.1.99.2) are found between trusted and noise cutoffs, but this model captures nearly all tryptophanases for which the leader peptide gene tnaC can be found upstream. [Energy metabolism, Amino acids and amines]
Pssm-ID: 131666 Cd Length: 467 Bit Score: 994.83 E-value: 0e+00
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ...
27-468
0e+00
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.
Pssm-ID: 99741 Cd Length: 431 Bit Score: 579.70 E-value: 0e+00
tryptophanase, leader peptide-associated; Members of this family belong to the ...
5-471
0e+00
tryptophanase, leader peptide-associated; Members of this family belong to the beta-eliminating lyase family (pfam01212) and act as tryptophanase (L-tryptophan indole-lyase). The tryptophanases of this family, as a rule, are found with a tryptophanase leader peptide (TnaC) encoded upstream. Both tryptophanases (4.1.99.1) and tyrosine phenol-lyases (EC 4.1.99.2) are found between trusted and noise cutoffs, but this model captures nearly all tryptophanases for which the leader peptide gene tnaC can be found upstream. [Energy metabolism, Amino acids and amines]
Pssm-ID: 131666 Cd Length: 467 Bit Score: 994.83 E-value: 0e+00
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ...
27-468
0e+00
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.
Pssm-ID: 99741 Cd Length: 431 Bit Score: 579.70 E-value: 0e+00
tyrosine phenol-lyase; This model describes a group of tyrosine phenol-lyase (4.1.99.2) ...
9-469
4.64e-170
tyrosine phenol-lyase; This model describes a group of tyrosine phenol-lyase (4.1.99.2) (beta-tyrosinase), a pyridoxal-phosphate enzyme closely related to tryptophanase (4.1.99.1) (see model TIGR02617). Both belong to the beta-eliminating lyase family (pfam01212) [Energy metabolism, Amino acids and amines]
Pssm-ID: 131667 Cd Length: 450 Bit Score: 485.96 E-value: 4.64e-170
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
80-283
1.69e-08
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 53.93 E-value: 1.69e-08
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
49-285
1.98e-06
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 49.64 E-value: 1.98e-06
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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