nucleotide-binding domain (NBD) of the butyrate kinase (BK) domain family; Butyrate kinase (EC ...
3-344
2.05e-150
nucleotide-binding domain (NBD) of the butyrate kinase (BK) domain family; Butyrate kinase (EC 2.7.2.7) catalyzes the formation of butyryl-CoA by phosphorylating butyrate in the presence of ATP to form butyryl phosphate. Butyrate kinases exist in many fermentative species of the bacterial and archaeal families. They belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466861 Cd Length: 345 Bit Score: 426.95 E-value: 2.05e-150
butyrate kinase; This model represents an enzyme family in which members are designated either ...
3-344
5.70e-113
butyrate kinase; This model represents an enzyme family in which members are designated either butryate kinase or branched-chain carboxylic acid kinase. The EC designation 2.7.2.7 describes an enzyme with relatively broad specificity; gene products whose context suggests a role in metabolism of aliphatic amino acids are likely to act as branched-chain carboxylic acid kinase. The gene typically found adjacent, ptb (phosphate butyryltransferase), likewise encodes an enzyme that may have a broad specificity that includes a role in aliphatic amino acid cabolism. [Energy metabolism, Fermentation]
Pssm-ID: 162981 Cd Length: 351 Bit Score: 332.44 E-value: 5.70e-113
nucleotide-binding domain (NBD) of the butyrate kinase (BK) domain family; Butyrate kinase (EC ...
3-344
2.05e-150
nucleotide-binding domain (NBD) of the butyrate kinase (BK) domain family; Butyrate kinase (EC 2.7.2.7) catalyzes the formation of butyryl-CoA by phosphorylating butyrate in the presence of ATP to form butyryl phosphate. Butyrate kinases exist in many fermentative species of the bacterial and archaeal families. They belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466861 Cd Length: 345 Bit Score: 426.95 E-value: 2.05e-150
butyrate kinase; This model represents an enzyme family in which members are designated either ...
3-344
5.70e-113
butyrate kinase; This model represents an enzyme family in which members are designated either butryate kinase or branched-chain carboxylic acid kinase. The EC designation 2.7.2.7 describes an enzyme with relatively broad specificity; gene products whose context suggests a role in metabolism of aliphatic amino acids are likely to act as branched-chain carboxylic acid kinase. The gene typically found adjacent, ptb (phosphate butyryltransferase), likewise encodes an enzyme that may have a broad specificity that includes a role in aliphatic amino acid cabolism. [Energy metabolism, Fermentation]
Pssm-ID: 162981 Cd Length: 351 Bit Score: 332.44 E-value: 5.70e-113
nucleotide-binding domain (NBD) of the acetate kinase (AcK)/propionate kinase (PK) domain ...
151-320
2.69e-15
nucleotide-binding domain (NBD) of the acetate kinase (AcK)/propionate kinase (PK) domain family; The family corresponds to a group of proteins which transfer phosphate from ATP to a short chain aliphatic acid. It includes acetate kinase (AckA) and propionate kinase (TdcD and PduW). Acetate kinase (EC 2.7.2.1), also called acetokinase, catalyzes the formation of acetyl phosphate from acetate and ATP. It can also catalyze the reverse reaction in the presence of a divalent cation. During anaerobic growth of the organism, this enzyme is also involved in the synthesis of most of the ATP formed catabolically. Propionate kinase TdcD (EC 2.7.2.15) catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor. The family also includes propionate kinase PduW (EC 2.7.2.15) that works with phosphate acetyltransferase (pta) to capture exogenous propionate and regenerate propionyl-CoA during degradation of propionate and 1,2-propanediol (1,2-PD). This protein restores growth to an eutQ deletion on ethanolamine and tetrathionate under anoxic conditions. The AcK/PK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466860 Cd Length: 392 Bit Score: 76.39 E-value: 2.69e-15
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.
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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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.
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,
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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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