Summary: ATP:guanido phosphotransferase, N-terminal domain
Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.
This is the Wikipedia entry entitled "ATP:guanido phosphotransferase family". More...
ATP:guanido phosphotransferase family Edit Wikipedia article
ATP:guanido phosphotransferase catalytic domain | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() structure of arginine kinase c271a mutant
|
|||||||||
Identifiers | |||||||||
Symbol | ATP-gua_Ptrans | ||||||||
Pfam | PF00217 | ||||||||
Pfam clan | CL0286 | ||||||||
InterPro | IPR022414 | ||||||||
PROSITE | PDOC00103 | ||||||||
SCOP | 1crk | ||||||||
SUPERFAMILY | 1crk | ||||||||
|
ATP:guanido phosphotransferase N-terminal domain | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() transition state structure of an arginine kinase mutant
|
|||||||||
Identifiers | |||||||||
Symbol | ATP-gua_PtransN | ||||||||
Pfam | PF02807 | ||||||||
InterPro | IPR022413 | ||||||||
PROSITE | PDOC00103 | ||||||||
SCOP | 1crk | ||||||||
SUPERFAMILY | 1crk | ||||||||
|
In molecular biology, the ATP:guanido phosphotransferase family is a family of structurally and functionally related enzymes,[1][2] that reversibly catalyse the transfer of phosphate between ATP and various phosphogens. The enzymes belonging to this family include:
- Glycocyamine kinase (EC 2.7.3.1), which catalyses the transfer of phosphate from ATP to guanidoacetate.
- Arginine kinase (EC 2.7.3.3), which catalyses the transfer of phosphate from ATP to arginine.
- Taurocyamine kinase (EC 2.7.3.4), an annelid-specific enzyme that catalyses the transfer of phosphate from ATP to taurocyamine.
- Lombricine kinase (EC 2.7.3.5), an annelid-specific enzyme that catalyses the transfer of phosphate from ATP to lombricine.
- Smc74, a cercaria-specific enzyme from Schistosoma mansoni.[1]
- Creatine kinase (EC 2.7.3.2) (CK),[3][4] which catalyses the reversible transfer of high energy phosphate from ATP to creatine, generating phosphocreatine and ADP.
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 mitochondrial. 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.[5] 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.[5] They also contain an N-terminal domain which has an all-alpha fold consisting of an irregular array of 6 short helices.[5]
References
- ^ a b Stein LD, Harn DA, David JR (April 1990). "A cloned ATP:guanidino kinase in the trematode Schistosoma mansoni has a novel duplicated structure". J. Biol. Chem. 265 (12): 6582–8. PMID 2324092.
- ^ Strong SJ, Ellington WR (January 1995). "Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues". Biochim. Biophys. Acta. 1246 (2): 197–200. doi:10.1016/0167-4838(94)00218-6. PMID 7819288.
- ^ Bessman SP, Carpenter CL (1985). "The creatine-creatine phosphate energy shuttle". Annu. Rev. Biochem. 54: 831–62. doi:10.1146/annurev.bi.54.070185.004151. PMID 3896131.
- ^ Haas RC, Strauss AW (April 1990). "Separate nuclear genes encode sarcomere-specific and ubiquitous human mitochondrial creatine kinase isoenzymes". J. Biol. Chem. 265 (12): 6921–7. PMID 2324105.
- ^ a b c Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W (May 1996). "Structure of mitochondrial creatine kinase". Nature. 381 (6580): 341–5. doi:10.1038/381341a0. PMID 8692275.
This article incorporates text from the public domain Pfam and InterPro IPR022413
This article incorporates text from the public domain Pfam and InterPro IPR022414
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
ATP:guanido phosphotransferase, N-terminal domain Provide feedback
The N-terminal domain has an all-alpha fold.
Literature references
-
Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W; , Nature 1996;381:341-345.: Structure of mitochondrial creatine kinase. PUBMED:8692275 EPMC:8692275
External database links
PROSITE: | PDOC00103 |
SCOP: | 1crk |
This tab holds annotation information from the InterPro database.
InterPro entry IPR022413
This entry represents the N-terminal domain of ATP:guanido phosphotransferase, which has an all-alpha fold consisting of an irregular array of 6 short helices [PUBMED:8692275].
ATP:guanido phosphotransferases are a family of structurally and functionally related enzymes [PUBMED:2324092, PUBMED:7819288] that reversibly catalyse the transfer of phosphate between ATP and various phosphogens. The enzymes belonging to this family include:
- Glycocyamine kinase (EC), which catalyses the transfer of phosphate from ATP to guanidoacetate.
- Arginine kinase (EC), which catalyses the transfer of phosphate from ATP to arginine.
- Taurocyamine kinase (EC), an annelid-specific enzyme that catalyses the transfer of phosphate from ATP to taurocyamine.
- Lombricine kinase (EC), an annelid-specific enzyme that catalyses the transfer of phosphate from ATP to lombricine.
- Smc74, a cercaria-specific enzyme from Schistosoma mansoni [PUBMED:2324092].
- Creatine kinase (EC) (CK) [PUBMED:3896131, PUBMED:2324105], which catalyses the reversible transfer of high energy phosphate from ATP to creatine, generating phosphocreatine and ADP.
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 mitochondrial. 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.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | kinase activity (GO:0016301) |
transferase activity, transferring phosphorus-containing groups (GO:0016772) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (88) |
Full (1735) |
Representative proteomes | UniProt (6032) |
NCBI (5847) |
Meta (21) |
||||
---|---|---|---|---|---|---|---|---|---|
RP15 (365) |
RP35 (660) |
RP55 (1281) |
RP75 (1812) |
||||||
Jalview | |||||||||
HTML | |||||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (88) |
Full (1735) |
Representative proteomes | UniProt (6032) |
NCBI (5847) |
Meta (21) |
||||
---|---|---|---|---|---|---|---|---|---|
RP15 (365) |
RP35 (660) |
RP55 (1281) |
RP75 (1812) |
||||||
Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Prosite |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Finn RD |
Number in seed: | 88 |
Number in full: | 1735 |
Average length of the domain: | 68.30 aa |
Average identity of full alignment: | 51 % |
Average coverage of the sequence by the domain: | 16.47 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
|
||||||||||||
Model details: |
|
||||||||||||
Model length: | 67 | ||||||||||||
Family (HMM) version: | 16 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
HideWeight segments by...
Change the size of the sunburst
Colour assignments
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
Selections
Align selected sequences to HMM
Generate a FASTA-format file
Clear selection
This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
Loading...
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ATP-gua_PtransN domain has been found. There are 144 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
Loading structure mapping...