phosphoserine transaminase catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine
phosphoserine aminotransferase, Methanosarcina type; This model represents a variant form of ...
10-383
0e+00
phosphoserine aminotransferase, Methanosarcina type; This model represents a variant form of the serine biosynthesis enzyme phosphoserine aminotransferase, as found in a small number of distantly related species, including Caulobacter crescentus, Mesorhizobium loti, and the archaeon Methanosarcina barkeri. [Amino acid biosynthesis, Serine family]
Pssm-ID: 130432 Cd Length: 374 Bit Score: 642.77 E-value: 0e+00
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
49-207
3.38e-35
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: 127.50 E-value: 3.38e-35
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and ...
10-317
5.24e-26
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and metabolism]; Phosphoserine aminotransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 441535 Cd Length: 358 Bit Score: 107.46 E-value: 5.24e-26
phosphoserine aminotransferase, Methanosarcina type; This model represents a variant form of ...
10-383
0e+00
phosphoserine aminotransferase, Methanosarcina type; This model represents a variant form of the serine biosynthesis enzyme phosphoserine aminotransferase, as found in a small number of distantly related species, including Caulobacter crescentus, Mesorhizobium loti, and the archaeon Methanosarcina barkeri. [Amino acid biosynthesis, Serine family]
Pssm-ID: 130432 Cd Length: 374 Bit Score: 642.77 E-value: 0e+00
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
49-207
3.38e-35
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: 127.50 E-value: 3.38e-35
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and ...
10-317
5.24e-26
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and metabolism]; Phosphoserine aminotransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 441535 Cd Length: 358 Bit Score: 107.46 E-value: 5.24e-26
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP) ...
40-317
4.68e-19
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major group in this CD corresponds to phosphoserine aminotransferase (PSAT). PSAT is active as a dimer and catalyzes the conversion of phosphohydroxypyruvate to phosphoserine.
Pssm-ID: 99736 [Multi-domain] Cd Length: 355 Bit Score: 87.35 E-value: 4.68e-19
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
20-313
4.84e-14
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 72.71 E-value: 4.84e-14
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
29-215
9.70e-13
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 68.96 E-value: 9.70e-13
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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Functional characterization of the conserved domain architecture found on the query.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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