acetyl-CoA carboxylase carboxyltransferase subunit beta (AccD) is a component of the acetyl coenzyme A carboxylase (ACC) complex that catalyzes the carboxylation of acetyl-CoA to form malonyl-CoA
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
1-281
0e+00
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase beta subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
:
Pssm-ID: 440540 [Multi-domain] Cd Length: 280 Bit Score: 558.14 E-value: 0e+00
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
1-281
0e+00
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase beta subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440540 [Multi-domain] Cd Length: 280 Bit Score: 558.14 E-value: 0e+00
acetyl-CoA carboxylase, carboxyl transferase, beta subunit; The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the beta chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129606 [Multi-domain] Cd Length: 285 Bit Score: 472.36 E-value: 8.11e-170
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
56-236
4.28e-15
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 75.37 E-value: 4.28e-15
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
1-281
0e+00
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase beta subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440540 [Multi-domain] Cd Length: 280 Bit Score: 558.14 E-value: 0e+00
acetyl-CoA carboxylase, carboxyl transferase, beta subunit; The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the beta chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129606 [Multi-domain] Cd Length: 285 Bit Score: 472.36 E-value: 8.11e-170
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
56-236
4.28e-15
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 75.37 E-value: 4.28e-15
Acetyl-coA carboxylase zinc finger domain; Acetyl-coA carboxylase (ACC) is a central metabolic ...
26-51
7.02e-11
Acetyl-coA carboxylase zinc finger domain; Acetyl-coA carboxylase (ACC) is a central metabolic enzyme that catalyzes the committed step in fatty acid biosynthesis: biotin- dependent conversion of acetyl-coA to malonyl-coA. In bacteria this protein contains a small zinc finger domain.
Pssm-ID: 436090 [Multi-domain] Cd Length: 26 Bit Score: 56.07 E-value: 7.02e-11
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.
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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,
for each region on the query sequence:
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
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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