Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]; ...
8-306
3.95e-137
Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]; Glutamate N-acetyltransferase (ornithine transacetylase) is part of the Pathway/BioSystem: Arginine biosynthesis
The actual alignment was detected with superfamily member COG1364:
Pssm-ID: 440975 Cd Length: 402 Bit Score: 393.64 E-value: 3.95e-137
Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]; ...
8-306
3.95e-137
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: 393.64 E-value: 3.95e-137
Ornithine acetyltransferase (OAT) family; also referred to as ArgJ. OAT catalyzes the first ...
8-306
1.01e-131
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: 379.50 E-value: 1.01e-131
glutamate N-acetyltransferase/amino-acid acetyltransferase; This enzyme can acetylate Glu to ...
4-306
6.25e-95
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: 286.33 E-value: 6.25e-95
Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]; ...
8-306
3.95e-137
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: 393.64 E-value: 3.95e-137
Ornithine acetyltransferase (OAT) family; also referred to as ArgJ. OAT catalyzes the first ...
8-306
1.01e-131
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: 379.50 E-value: 1.01e-131
glutamate N-acetyltransferase/amino-acid acetyltransferase; This enzyme can acetylate Glu to ...
4-306
6.25e-95
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: 286.33 E-value: 6.25e-95
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
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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Domains are color coded according to superfamilies
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superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
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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
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
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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