biotin--[acetyl-CoA-carboxylase] ligase catalyzes the formation of biotinyl-5'-AMP from biotin and ATP, and the succeeding biotinylation of the biotin carboxyl carrier protein
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
8-210
1.49e-38
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis
:
Pssm-ID: 440109 [Multi-domain] Cd Length: 241 Bit Score: 132.99 E-value: 1.49e-38
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
8-210
1.49e-38
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 440109 [Multi-domain] Cd Length: 241 Bit Score: 132.99 E-value: 1.49e-38
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
2-150
2.10e-21
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine.
Pssm-ID: 319741 [Multi-domain] Cd Length: 173 Bit Score: 86.55 E-value: 2.10e-21
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
14-209
7.99e-18
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the biotin--acetyl-CoA-carboxylase ligase region of biotin--acetyl-CoA-carboxylase ligase. In Escherichia coli and some other species, this enzyme is part of a bifunction protein BirA that includes a small, N-terminal biotin operon repressor domain. Proteins identified by this model should not be called bifunctional unless they are also identified by birA_repr_reg (TIGR00122). The protein name suggests that this enzyme transfers biotin only to acetyl-CoA-carboxylase but it also transfers the biotin moiety to other proteins. The apparent orthologs among the eukaryotes are larger proteins that contain a single copy of this domain. [Protein fate, Protein modification and repair]
Pssm-ID: 272917 [Multi-domain] Cd Length: 237 Bit Score: 78.60 E-value: 7.99e-18
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
167-209
2.46e-04
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It is found to the C terminus of the biotin protein ligase catalytic domain pfam01317.
Pssm-ID: 426672 [Multi-domain] Cd Length: 48 Bit Score: 37.44 E-value: 2.46e-04
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
8-210
1.49e-38
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 440109 [Multi-domain] Cd Length: 241 Bit Score: 132.99 E-value: 1.49e-38
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
2-150
2.10e-21
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine.
Pssm-ID: 319741 [Multi-domain] Cd Length: 173 Bit Score: 86.55 E-value: 2.10e-21
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
14-209
7.99e-18
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the biotin--acetyl-CoA-carboxylase ligase region of biotin--acetyl-CoA-carboxylase ligase. In Escherichia coli and some other species, this enzyme is part of a bifunction protein BirA that includes a small, N-terminal biotin operon repressor domain. Proteins identified by this model should not be called bifunctional unless they are also identified by birA_repr_reg (TIGR00122). The protein name suggests that this enzyme transfers biotin only to acetyl-CoA-carboxylase but it also transfers the biotin moiety to other proteins. The apparent orthologs among the eukaryotes are larger proteins that contain a single copy of this domain. [Protein fate, Protein modification and repair]
Pssm-ID: 272917 [Multi-domain] Cd Length: 237 Bit Score: 78.60 E-value: 7.99e-18
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
167-209
2.46e-04
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It is found to the C terminus of the biotin protein ligase catalytic domain pfam01317.
Pssm-ID: 426672 [Multi-domain] Cd Length: 48 Bit Score: 37.44 E-value: 2.46e-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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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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Others (non-specific hits) and
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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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