polyphosphate kinase 2 (PPK2) family protein similar to bacteria PPK2 that catalyzes the polyP-dependent phosphorylation of nucleoside diphosphates (ADP, GDP) to nucleoside triphosphates
polyphosphate:nucleotide phosphotransferase, PPK2 family; Members of this protein family ...
5-282
2.14e-160
polyphosphate:nucleotide phosphotransferase, PPK2 family; Members of this protein family belong to the polyphosphate kinase 2 (PPK2) family, which is not related in sequence to PPK1. While PPK1 tends to act in the biosynthesis of polyphosphate, or poly(P), members of the PPK2 family tend to use the terminal phosphate of poly(P) to regenerate ATP or GTP from the corresponding nucleoside diphosphate, or ADP from AMP as is the case with polyphosphate:AMP phosphotransferase (PAP). Members of this protein family most likely transfer the terminal phosphate between poly(P) and some nucleotide, but it is not clear which. [Central intermediary metabolism, Phosphorus compounds]
:
Pssm-ID: 274737 Cd Length: 264 Bit Score: 446.64 E-value: 2.14e-160
polyphosphate:nucleotide phosphotransferase, PPK2 family; Members of this protein family ...
5-282
2.14e-160
polyphosphate:nucleotide phosphotransferase, PPK2 family; Members of this protein family belong to the polyphosphate kinase 2 (PPK2) family, which is not related in sequence to PPK1. While PPK1 tends to act in the biosynthesis of polyphosphate, or poly(P), members of the PPK2 family tend to use the terminal phosphate of poly(P) to regenerate ATP or GTP from the corresponding nucleoside diphosphate, or ADP from AMP as is the case with polyphosphate:AMP phosphotransferase (PAP). Members of this protein family most likely transfer the terminal phosphate between poly(P) and some nucleotide, but it is not clear which. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 274737 Cd Length: 264 Bit Score: 446.64 E-value: 2.14e-160
Polyphosphate kinase 2 (PPK2); Inorganic polyphosphate (polyP) plays a role in metabolism and ...
30-264
1.18e-69
Polyphosphate kinase 2 (PPK2); Inorganic polyphosphate (polyP) plays a role in metabolism and regulation and has been proposed to serve as a energy source in a pre-ATP world. In prokaryotes, the synthesis and utilization of polyP are catalyzed by PPK1, PPK2 and polyphosphatases. Proteins with a single PPK2 domain catalyze polyP-dependent phosphorylation of ADP to ATP, whereas proteins containing 2 fused PPK2 domains phosphorylate AMP to ADP. The structure of PPK2 from Pseudomonas aeruginosa has revealed a a 3-layer alpha/beta/alpha sandwich fold with an alpha-helical lid similar to the structures of microbial thymidylate kinases.
Pssm-ID: 397878 Cd Length: 229 Bit Score: 215.34 E-value: 1.18e-69
polyphosphate:nucleotide phosphotransferase, PPK2 family; Members of this protein family ...
5-282
2.14e-160
polyphosphate:nucleotide phosphotransferase, PPK2 family; Members of this protein family belong to the polyphosphate kinase 2 (PPK2) family, which is not related in sequence to PPK1. While PPK1 tends to act in the biosynthesis of polyphosphate, or poly(P), members of the PPK2 family tend to use the terminal phosphate of poly(P) to regenerate ATP or GTP from the corresponding nucleoside diphosphate, or ADP from AMP as is the case with polyphosphate:AMP phosphotransferase (PAP). Members of this protein family most likely transfer the terminal phosphate between poly(P) and some nucleotide, but it is not clear which. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 274737 Cd Length: 264 Bit Score: 446.64 E-value: 2.14e-160
Polyphosphate kinase 2 (PPK2); Inorganic polyphosphate (polyP) plays a role in metabolism and ...
30-264
1.18e-69
Polyphosphate kinase 2 (PPK2); Inorganic polyphosphate (polyP) plays a role in metabolism and regulation and has been proposed to serve as a energy source in a pre-ATP world. In prokaryotes, the synthesis and utilization of polyP are catalyzed by PPK1, PPK2 and polyphosphatases. Proteins with a single PPK2 domain catalyze polyP-dependent phosphorylation of ADP to ATP, whereas proteins containing 2 fused PPK2 domains phosphorylate AMP to ADP. The structure of PPK2 from Pseudomonas aeruginosa has revealed a a 3-layer alpha/beta/alpha sandwich fold with an alpha-helical lid similar to the structures of microbial thymidylate kinases.
Pssm-ID: 397878 Cd Length: 229 Bit Score: 215.34 E-value: 1.18e-69
polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain ...
43-264
1.21e-50
polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain duplication. The characterized member from Acinetobacter johnsonii is polyphosphate:AMP phosphotransferase (PAP), which can transfer the terminal phosphate from poly(P) to AMP, yielding ADP. In the opposite direction, this enzyme can synthesize poly(P). Each domain of this protein family is homologous to polyphosphate kinase, an enzyme that can run in the forward direction to extend a polyphosphate chain with a new terminal phosphate from ATP, or in reverse to make ATP (or GTP) from ADP (or GDP). [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 274736 [Multi-domain] Cd Length: 493 Bit Score: 173.68 E-value: 1.21e-50
polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain ...
30-290
7.30e-42
polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain duplication. The characterized member from Acinetobacter johnsonii is polyphosphate:AMP phosphotransferase (PAP), which can transfer the terminal phosphate from poly(P) to AMP, yielding ADP. In the opposite direction, this enzyme can synthesize poly(P). Each domain of this protein family is homologous to polyphosphate kinase, an enzyme that can run in the forward direction to extend a polyphosphate chain with a new terminal phosphate from ATP, or in reverse to make ATP (or GTP) from ADP (or GDP). [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 274736 [Multi-domain] Cd Length: 493 Bit Score: 150.57 E-value: 7.30e-42
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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