ATP--guanido phosphotransferase reversibly catalyzes the transfer of phosphate between ATP and various phosphogens; similar to Arenicola marina taurocyamine kinase that catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate)
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
4-247
5.56e-174
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK). The majority of bacterial phosphagen kinases appear to lack the N-terminal domain and have not been functionally characterized.
The actual alignment was detected with superfamily member cd00716:
Pssm-ID: 470681 [Multi-domain] Cd Length: 357 Bit Score: 483.38 E-value: 5.56e-174
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
4-247
5.56e-174
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic creatine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CKs are found as tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial, cytosolic, and flagellar) isoforms. Mitochondrial and cytoplasmic CKs are dimeric or octameric, while the flagellar isoforms are trimers with three CD domains fused as a single protein chain. CKs are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK, one of the most studied members of this family, this model also represents other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK), and echinoderm arginine kinase (AK).
Pssm-ID: 153076 [Multi-domain] Cd Length: 357 Bit Score: 483.38 E-value: 5.56e-174
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
34-241
8.19e-112
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is located in the cleft between N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain.
Pssm-ID: 459716 Cd Length: 203 Bit Score: 319.87 E-value: 8.19e-112
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
4-247
5.56e-174
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic creatine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CKs are found as tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial, cytosolic, and flagellar) isoforms. Mitochondrial and cytoplasmic CKs are dimeric or octameric, while the flagellar isoforms are trimers with three CD domains fused as a single protein chain. CKs are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK, one of the most studied members of this family, this model also represents other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK), and echinoderm arginine kinase (AK).
Pssm-ID: 153076 [Multi-domain] Cd Length: 357 Bit Score: 483.38 E-value: 5.56e-174
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
5-240
1.13e-117
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK).
Pssm-ID: 153078 [Multi-domain] Cd Length: 338 Bit Score: 340.02 E-value: 1.13e-117
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
34-241
8.19e-112
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is located in the cleft between N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain.
Pssm-ID: 459716 Cd Length: 203 Bit Score: 319.87 E-value: 8.19e-112
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
4-240
5.51e-111
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK). The majority of bacterial phosphagen kinases appear to lack the N-terminal domain and have not been functionally characterized.
Pssm-ID: 153075 Cd Length: 236 Bit Score: 319.15 E-value: 5.51e-111
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
3-241
1.76e-92
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic arginine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphoarginine in the case of arginine kinase (AK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. Besides AK, one of the most studied members of this family, this model also represents a phosphagen kinase with different substrate specificity, hypotaurocyamine kinase (HTK).
Pssm-ID: 153079 [Multi-domain] Cd Length: 350 Bit Score: 276.50 E-value: 1.76e-92
Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes ...
4-240
1.21e-31
Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, such as phosphocreatine (PCr) or phosphoarginine, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. This subfamily is specific to bacteria and lacks an N-terminal domain, which otherwise forms part of the substrate binding site. Most of the catalytic residues are found in the larger C-terminal domain, however, which appears conserved in these bacterial proteins. Their functions have not been characterized.
Pssm-ID: 153077 Cd Length: 232 Bit Score: 116.46 E-value: 1.21e-31
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.
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