Homoserine O-succinyltransferase [Amino acid transport and metabolism]; Homoserine ...
1-309
0e+00
Homoserine O-succinyltransferase [Amino acid transport and metabolism]; Homoserine O-succinyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 441501 Cd Length: 309 Bit Score: 573.96 E-value: 0e+00
Homoserine O-succinyltransferase; The activation of homoserine through succinylation of ...
2-299
0e+00
Homoserine O-succinyltransferase; The activation of homoserine through succinylation of homoserine in some bacteria, such as Escherichia coli and Bacillus cereus, is carried out by homoserine O-succinyltransferase (HTS, EC:2.3.1.46), while other bacteria, such as Haemophilus influenzae, Pseudomonas aeruginosa, and Mycobacterium tuberculosis, acetylate homoserine via homoserine O-acetyltransferase (HTA;EC:2.3.1.31). This family also includes serine acetyltransferase CysE (EC:2.3.1.30) from Lactobacillus casei, which catalyzes the formation of O-acetyl serine from L-serine and acetyl-CoA, and is involved in cysteine biosynthesis.
Pssm-ID: 427782 [Multi-domain] Cd Length: 298 Bit Score: 532.52 E-value: 0e+00
homoserine O-succinyltransferase; The apparent equivalog from Bacillus subtilis is broken into ...
1-301
6.13e-175
homoserine O-succinyltransferase; The apparent equivalog from Bacillus subtilis is broken into two tandem reading frames. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 130074 Cd Length: 300 Bit Score: 485.89 E-value: 6.13e-175
Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase ...
38-212
8.94e-82
Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase (HTS); Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase (HTS). HTS, the first enzyme in methionine biosynthesis in Escherichia coli, transfers a succinyl group from succinyl-CoA to homoserine forming succinyl homoserine. It has been suggested that the succinyl group of succinyl-CoA is initially transferred to an enzyme nucleophile before subsequent transfer to homoserine. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with GATase1 domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. It has been proposed that this cys is in the active site of the molecule. However, as succinyl has been found bound to a conserved lysine residue, this conserved cys may play a role in dimer formation. HTS activity is tightly regulated by several mechanisms including feedback inhibition and proteolysis. It represents a critical control point for cell growth and viability.
Pssm-ID: 153225 Cd Length: 175 Bit Score: 244.86 E-value: 8.94e-82
Homoserine O-succinyltransferase [Amino acid transport and metabolism]; Homoserine ...
1-309
0e+00
Homoserine O-succinyltransferase [Amino acid transport and metabolism]; Homoserine O-succinyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 441501 Cd Length: 309 Bit Score: 573.96 E-value: 0e+00
Homoserine O-succinyltransferase; The activation of homoserine through succinylation of ...
2-299
0e+00
Homoserine O-succinyltransferase; The activation of homoserine through succinylation of homoserine in some bacteria, such as Escherichia coli and Bacillus cereus, is carried out by homoserine O-succinyltransferase (HTS, EC:2.3.1.46), while other bacteria, such as Haemophilus influenzae, Pseudomonas aeruginosa, and Mycobacterium tuberculosis, acetylate homoserine via homoserine O-acetyltransferase (HTA;EC:2.3.1.31). This family also includes serine acetyltransferase CysE (EC:2.3.1.30) from Lactobacillus casei, which catalyzes the formation of O-acetyl serine from L-serine and acetyl-CoA, and is involved in cysteine biosynthesis.
Pssm-ID: 427782 [Multi-domain] Cd Length: 298 Bit Score: 532.52 E-value: 0e+00
homoserine O-succinyltransferase; The apparent equivalog from Bacillus subtilis is broken into ...
1-301
6.13e-175
homoserine O-succinyltransferase; The apparent equivalog from Bacillus subtilis is broken into two tandem reading frames. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 130074 Cd Length: 300 Bit Score: 485.89 E-value: 6.13e-175
Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase ...
38-212
8.94e-82
Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase (HTS); Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase (HTS). HTS, the first enzyme in methionine biosynthesis in Escherichia coli, transfers a succinyl group from succinyl-CoA to homoserine forming succinyl homoserine. It has been suggested that the succinyl group of succinyl-CoA is initially transferred to an enzyme nucleophile before subsequent transfer to homoserine. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with GATase1 domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. It has been proposed that this cys is in the active site of the molecule. However, as succinyl has been found bound to a conserved lysine residue, this conserved cys may play a role in dimer formation. HTS activity is tightly regulated by several mechanisms including feedback inhibition and proteolysis. It represents a critical control point for cell growth and viability.
Pssm-ID: 153225 Cd Length: 175 Bit Score: 244.86 E-value: 8.94e-82
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.
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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,
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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,
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specific hits meet or exceed a domain-specific e-value threshold
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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
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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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