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*Now available with Java™ 1.5!*
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| Family: |
ARGININE OR CREATINE KINASE (PTHR11547)
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| Subfamilies: |
8
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| PANTHER Links: |
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| Abstract: |
ATP:guanido phosphotransferases are a family of structurally and functionally related enzymes
[PMID:2324092, PMID:7819288] that reversibly catalyze the transfer of phosphate between
ATP and various phosphogens. The enzymes belonging to this family include glycocyamine kinase
(EC: 2.7.3.1), which catalyzes the transfer of phosphate from ATP to guanidoacetate; arginine
kinase (EC: 2.7.3.3), which catalyzes the transfer of phosphate from ATP to arginine; taurocyamine
kinase (EC: 2.7.3.4), an annelid-specific enzyme that catalyzes the transfer of phosphate from ATP
to taurocyamine; lombricine kinase (EC: 2.7.3.5), an annelid-specific enzyme that catalyzes the
transfer of phosphate from ATP to lombricine; Smc74, a cercaria-specific enzyme from Schistosoma
mansoni [PMID:2324092]; and creatine kinase (EC: 2.7.3.2) (CK) [PMID:3896131, PMID:2324105], which plays an important role in energy metabolism of vertebrates. It catalyzes the
reversible transfer of high energy phosphate from ATP to creatine, generating phosphocreatine and
ADP. 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 mitochondrial. In sea urchin 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.
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| InterPro Accession: |
IPR000749
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| PANTHER Molecular Function: |
Molecular function unclassified
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| PANTHER Biological Process: |
Biological process unclassified
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| Pathway Categories: |
No pathway information available
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| Training Sequences: |
72
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| HMM Length |
325
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| Downloads: |
HMM (HMMER format) |
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Total |
Celera |
FlyBase |
NCBI |
| H. sapiens |
12
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5
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0 |
7
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| M. musculus |
11
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6
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0 |
5
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| R. norvegicus |
7
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4
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0 |
3
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| D. melanogaster |
4
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0 |
4
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0 |
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