polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain ...
14-471
3.79e-150
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]
The actual alignment was detected with superfamily member TIGR03708:
Pssm-ID: 274736 [Multi-domain] Cd Length: 493 Bit Score: 436.78 E-value: 3.79e-150
polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain ...
14-471
3.79e-150
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: 436.78 E-value: 3.79e-150
Polyphosphate kinase 2 (PPK2); Inorganic polyphosphate (polyP) plays a role in metabolism and ...
252-472
8.81e-82
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: 252.71 E-value: 8.81e-82
polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain ...
14-471
3.79e-150
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: 436.78 E-value: 3.79e-150
Polyphosphate kinase 2 (PPK2); Inorganic polyphosphate (polyP) plays a role in metabolism and ...
252-472
8.81e-82
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: 252.71 E-value: 8.81e-82
polyphosphate:nucleotide phosphotransferase, PPK2 family; Members of this protein family ...
254-470
3.04e-64
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: 208.59 E-value: 3.04e-64
polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain ...
253-471
7.40e-55
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: 190.63 E-value: 7.40e-55
Polyphosphate kinase 2 (PPK2); Inorganic polyphosphate (polyP) plays a role in metabolism and ...
11-224
3.85e-14
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: 71.66 E-value: 3.85e-14
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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