carboxyltransferase domain-containing protein catalyzes the transcarboxylation from biotin to an acyl-CoA acceptor molecule; similar to methylcrotonyl-CoA carboxylase subunit beta
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
36-563
0e+00
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.
The actual alignment was detected with superfamily member PLN02820:
Pssm-ID: 481543 [Multi-domain] Cd Length: 569 Bit Score: 895.70 E-value: 0e+00
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
77-554
1.25e-178
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: 512.96 E-value: 1.25e-178
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
77-554
1.25e-178
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: 512.96 E-value: 1.25e-178
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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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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