PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
1-150
1.46e-77
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).
The actual alignment was detected with superfamily member PRK00062:
Pssm-ID: 450240 [Multi-domain] Cd Length: 426 Bit Score: 236.12 E-value: 1.46e-77
Glutamate-1-semialdehyde aminotransferase [Coenzyme transport and metabolism]; ...
1-152
3.95e-72
Glutamate-1-semialdehyde aminotransferase [Coenzyme transport and metabolism]; Glutamate-1-semialdehyde aminotransferase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439772 [Multi-domain] Cd Length: 429 Bit Score: 222.23 E-value: 3.95e-72
glutamate-1-semialdehyde-2,1-aminomutase; This enzyme, glutamate-1-semialdehyde-2, ...
1-149
5.68e-57
glutamate-1-semialdehyde-2,1-aminomutase; This enzyme, glutamate-1-semialdehyde-2,1-aminomutase (glutamate-1-semialdehyde aminotransferase, GSA aminotransferase), contains a pyridoxal phosphate attached at a Lys residue at position 283 of the seed alignment. It is in the family of class III aminotransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273230 [Multi-domain] Cd Length: 423 Bit Score: 183.33 E-value: 5.68e-57
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
5-146
2.61e-26
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.
Pssm-ID: 99735 [Multi-domain] Cd Length: 413 Bit Score: 102.26 E-value: 2.61e-26
Glutamate-1-semialdehyde aminotransferase [Coenzyme transport and metabolism]; ...
1-152
3.95e-72
Glutamate-1-semialdehyde aminotransferase [Coenzyme transport and metabolism]; Glutamate-1-semialdehyde aminotransferase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439772 [Multi-domain] Cd Length: 429 Bit Score: 222.23 E-value: 3.95e-72
glutamate-1-semialdehyde-2,1-aminomutase; This enzyme, glutamate-1-semialdehyde-2, ...
1-149
5.68e-57
glutamate-1-semialdehyde-2,1-aminomutase; This enzyme, glutamate-1-semialdehyde-2,1-aminomutase (glutamate-1-semialdehyde aminotransferase, GSA aminotransferase), contains a pyridoxal phosphate attached at a Lys residue at position 283 of the seed alignment. It is in the family of class III aminotransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273230 [Multi-domain] Cd Length: 423 Bit Score: 183.33 E-value: 5.68e-57
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
5-146
2.61e-26
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.
Pssm-ID: 99735 [Multi-domain] Cd Length: 413 Bit Score: 102.26 E-value: 2.61e-26
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
97-148
8.78e-05
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 41.19 E-value: 8.78e-05
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase [Coenzyme transport and metabolism]; ...
15-149
5.46e-04
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase [Coenzyme transport and metabolism]; Adenosylmethionine-8-amino-7-oxononanoate aminotransferase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439931 [Multi-domain] Cd Length: 446 Bit Score: 38.88 E-value: 5.46e-04
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
107-146
7.63e-03
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 35.61 E-value: 7.63e-03
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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