bifunctional ornithine acetyltransferase/N-acetylglutamate synthase catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate
Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]; ...
48-465
1.98e-153
Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]; Glutamate N-acetyltransferase (ornithine transacetylase) is part of the Pathway/BioSystem: Arginine biosynthesis
:
Pssm-ID: 440975 Cd Length: 402 Bit Score: 441.41 E-value: 1.98e-153
Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]; ...
48-465
1.98e-153
Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]; Glutamate N-acetyltransferase (ornithine transacetylase) is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440975 Cd Length: 402 Bit Score: 441.41 E-value: 1.98e-153
Ornithine acetyltransferase (OAT) family; also referred to as ArgJ. OAT catalyzes the first ...
50-465
1.50e-149
Ornithine acetyltransferase (OAT) family; also referred to as ArgJ. OAT catalyzes the first and fifth steps in arginine biosynthesis, coupling acetylation of glutamate with deacetylation of N-acetylornithine, which allows recycling of the acetyl group in the arginine biosynthetic pathway. Members of this family may experience feedback inhibition by L-arginine. The active enzyme is a heterotetramer of two alpha and two beta chains, where the alpha and beta chains are the result of autocatalytic cleavage. OATs found in the clavulanic acid biosynthesis gene cluster catalyze the fifth step only, and may utilize acetyl acceptors other than glutamate.
Pssm-ID: 239065 Cd Length: 390 Bit Score: 431.12 E-value: 1.50e-149
glutamate N-acetyltransferase/amino-acid acetyltransferase; This enzyme can acetylate Glu to ...
87-465
2.91e-91
glutamate N-acetyltransferase/amino-acid acetyltransferase; This enzyme can acetylate Glu to N-acetyl-Glu by deacetylating N-2-acetyl-ornithine into ornithine; the two halves of this reaction represent the first and fifth steps in the synthesis of Arg (or citrulline) from Glu by way of ornithine (EC 2.3.1.35). In Bacillus stearothermophilus, but not in Thermus thermophilus HB27, the enzyme is bifunctional and can also use acetyl-CoA to acetylate Glu (EC 2.3.1.1). [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 161718 Cd Length: 404 Bit Score: 282.86 E-value: 2.91e-91
Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]; ...
48-465
1.98e-153
Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]; Glutamate N-acetyltransferase (ornithine transacetylase) is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440975 Cd Length: 402 Bit Score: 441.41 E-value: 1.98e-153
Ornithine acetyltransferase (OAT) family; also referred to as ArgJ. OAT catalyzes the first ...
50-465
1.50e-149
Ornithine acetyltransferase (OAT) family; also referred to as ArgJ. OAT catalyzes the first and fifth steps in arginine biosynthesis, coupling acetylation of glutamate with deacetylation of N-acetylornithine, which allows recycling of the acetyl group in the arginine biosynthetic pathway. Members of this family may experience feedback inhibition by L-arginine. The active enzyme is a heterotetramer of two alpha and two beta chains, where the alpha and beta chains are the result of autocatalytic cleavage. OATs found in the clavulanic acid biosynthesis gene cluster catalyze the fifth step only, and may utilize acetyl acceptors other than glutamate.
Pssm-ID: 239065 Cd Length: 390 Bit Score: 431.12 E-value: 1.50e-149
glutamate N-acetyltransferase/amino-acid acetyltransferase; This enzyme can acetylate Glu to ...
87-465
2.91e-91
glutamate N-acetyltransferase/amino-acid acetyltransferase; This enzyme can acetylate Glu to N-acetyl-Glu by deacetylating N-2-acetyl-ornithine into ornithine; the two halves of this reaction represent the first and fifth steps in the synthesis of Arg (or citrulline) from Glu by way of ornithine (EC 2.3.1.35). In Bacillus stearothermophilus, but not in Thermus thermophilus HB27, the enzyme is bifunctional and can also use acetyl-CoA to acetylate Glu (EC 2.3.1.1). [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 161718 Cd Length: 404 Bit Score: 282.86 E-value: 2.91e-91
DmpA/OAT superfamily; composed of L-aminopeptidase D-amidase/D-esterase (DmpA), ornithine ...
69-304
9.13e-04
DmpA/OAT superfamily; composed of L-aminopeptidase D-amidase/D-esterase (DmpA), ornithine acetyltransferase (OAT) and similar proteins. DmpA is an aminopeptidase that releases N-terminal D and L amino acids from peptide substrates. This group represents one of the rare aminopeptidases that are not metalloenzymes. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine. OAT catalyzes the first and fifth steps in arginine biosynthesis, coupling acetylation of glutamate with deacetylation of N-acetylornithine, which allows recycling of the acetyl group in the arginine biosynthetic pathway. The superfamily also contains an enzyme, endo-type 6-aminohexanoate-oligomer hydrolase, that have been shown to be involved in nylon degradation. Proteins in this superfamily undergo autocatalytic cleavage of an inactive precursor at the site immediately upstream to the catalytic nucleophile.
Pssm-ID: 238070 Cd Length: 286 Bit Score: 41.23 E-value: 9.13e-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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(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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