ATP:guanido phosphotransferase family
| ATP:guanido phosphotransferase catalytic domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
structure of arginine kinase c271a mutant
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| Identifiers | |||||||||
| Symbol | ATP-gua_Ptrans | ||||||||
| Pfam | PF00217 | ||||||||
| Pfam clan | CL0286 | ||||||||
| InterPro | IPR022414 | ||||||||
| PROSITE | PDOC00103 | ||||||||
| SCOP | 1crk | ||||||||
| SUPERFAMILY | 1crk | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
| ATP:guanido phosphotransferase N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
transition state structure of an arginine kinase mutant
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| Identifiers | |||||||||
| Symbol | ATP-gua_PtransN | ||||||||
| Pfam | PF02807 | ||||||||
| InterPro | IPR022413 | ||||||||
| PROSITE | PDOC00103 | ||||||||
| SCOP | 1crk | ||||||||
| SUPERFAMILY | 1crk | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
In molecular biology, the ATP:guanido phosphotransferase family is a family of structurally and functionally related enzymes, that reversibly catalyse the transfer of phosphate between ATP and various phosphogens. The enzymes belonging to this family include:
Creatine kinase plays an important role in energy metabolism of vertebrates. There are at least four different, but very closely related, forms of CK. Two isozymes, M (muscle) and B (brain), are cytosolic, while the other two are . In sea urchins there is a flagellar isozyme, which consists of the triplication of a CK-domain. A cysteine residue is implicated in the catalytic activity of these enzymes and the region around this active site residue is highly conserved.
ATP:guanido phosphotransferases contain a C-terminal catalytic domain which consists of a duplication where the common core consists of two beta-alpha-beta2-alpha repeats. 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. They also contain an N-terminal domain which has an all-alpha fold consisting of an irregular array of 6 short helices.
This article incorporates text from the public domain Pfam and InterPro IPR022413
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