polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain ...
2-575
5.81e-164
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: 476.07 E-value: 5.81e-164
polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain ...
2-575
5.81e-164
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: 476.07 E-value: 5.81e-164
Polyphosphate kinase 2 (PPK2); Inorganic polyphosphate (polyP) plays a role in metabolism and ...
352-577
1.39e-87
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: 270.81 E-value: 1.39e-87
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
382-569
1.13e-07
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
Pssm-ID: 238835 Cd Length: 200 Bit Score: 52.27 E-value: 1.13e-07
polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain ...
2-575
5.81e-164
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: 476.07 E-value: 5.81e-164
Polyphosphate kinase 2 (PPK2); Inorganic polyphosphate (polyP) plays a role in metabolism and ...
352-577
1.39e-87
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: 270.81 E-value: 1.39e-87
polyphosphate:AMP phosphotransferase; Members of this protein family contain a domain ...
343-577
1.12e-64
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: 219.52 E-value: 1.12e-64
polyphosphate kinase 2, PA0141 family; Members of this protein family are designated ...
352-571
5.80e-58
polyphosphate kinase 2, PA0141 family; Members of this protein family are designated polyphosphate kinase 2 (PPK2) after the characterized protein in Pseudomonas aeruginosa. This family comprises one of three well-separated clades in the larger family described by pfam03976. PA0141 from this family has been shown capable of operating in reverse, with GDP preferred (over ADP) as a substrate, producing GTP (or ATP) by transfer of a phosphate residue from polyphosphate. Most species with a member of this family also encode a polyphosphate kinase 1 (PPK1). [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 213852 Cd Length: 230 Bit Score: 193.61 E-value: 5.80e-58
Polyphosphate kinase 2 (PPK2); Inorganic polyphosphate (polyP) plays a role in metabolism and ...
12-270
7.67e-31
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: 120.20 E-value: 7.67e-31
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
382-569
1.13e-07
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
Pssm-ID: 238835 Cd Length: 200 Bit Score: 52.27 E-value: 1.13e-07
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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