3-phosphoserine/phosphohydroxythreonine transaminase catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and ...
2-359
0e+00
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: 646.74 E-value: 0e+00
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP) ...
5-357
0e+00
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: 552.28 E-value: 0e+00
phosphoserine aminotransferase; This model represents the common form of the phosphoserine ...
12-359
0e+00
phosphoserine aminotransferase; This model represents the common form of the phosphoserine aminotransferase SerC. The phosphoserine aminotransferase of the archaeon Methanosarcina barkeri and putative phosphoserine aminotransferase of Mycobacterium tuberculosis are represented by separate models. All are members of the class V aminotransferases (pfam00266). [Amino acid biosynthesis, Serine family]
Pssm-ID: 130431 Cd Length: 349 Bit Score: 545.72 E-value: 0e+00
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and ...
2-359
0e+00
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: 646.74 E-value: 0e+00
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP) ...
5-357
0e+00
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: 552.28 E-value: 0e+00
phosphoserine aminotransferase; This model represents the common form of the phosphoserine ...
12-359
0e+00
phosphoserine aminotransferase; This model represents the common form of the phosphoserine aminotransferase SerC. The phosphoserine aminotransferase of the archaeon Methanosarcina barkeri and putative phosphoserine aminotransferase of Mycobacterium tuberculosis are represented by separate models. All are members of the class V aminotransferases (pfam00266). [Amino acid biosynthesis, Serine family]
Pssm-ID: 130431 Cd Length: 349 Bit Score: 545.72 E-value: 0e+00
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
7-294
5.89e-04
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: 41.51 E-value: 5.89e-04
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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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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