Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
1-293
2.35e-176
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
The actual alignment was detected with superfamily member TIGR01001:
Pssm-ID: 469582 Cd Length: 300 Bit Score: 488.59 E-value: 2.35e-176
homoserine O-succinyltransferase; The apparent equivalog from Bacillus subtilis is broken into ...
1-293
2.35e-176
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: 488.59 E-value: 2.35e-176
Homoserine O-succinyltransferase; The activation of homoserine through succinylation of ...
2-291
1.73e-159
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: 445.85 E-value: 1.73e-159
Homoserine O-succinyltransferase [Amino acid transport and metabolism]; Homoserine ...
1-293
8.74e-149
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: 419.11 E-value: 8.74e-149
Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase ...
37-212
2.76e-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: 245.63 E-value: 2.76e-82
homoserine O-succinyltransferase; The apparent equivalog from Bacillus subtilis is broken into ...
1-293
2.35e-176
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: 488.59 E-value: 2.35e-176
Homoserine O-succinyltransferase; The activation of homoserine through succinylation of ...
2-291
1.73e-159
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: 445.85 E-value: 1.73e-159
Homoserine O-succinyltransferase [Amino acid transport and metabolism]; Homoserine ...
1-293
8.74e-149
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: 419.11 E-value: 8.74e-149
Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase ...
37-212
2.76e-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: 245.63 E-value: 2.76e-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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