Summary: ATP:guanido phosphotransferase, N-terminal domain

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Wikipedia: ATP:guanido phosphotransferase family
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ATP:guanido phosphotransferase family Edit Wikipedia article

ATP:guanido phosphotransferase catalytic domain

structure of arginine kinase c271a mutant

Identifiers

Symbol

ATP-gua_Ptrans

Pfam clan

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

Identifiers

Symbol

ATP-gua_PtransN

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,^[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...

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Alignments

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There are various ways to view or download the sequence alignments that we store. We provide several sequence viewers and a plain-text Stockholm-format file for download.

Alignment types

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RP15/RP35/RP55/RP75: Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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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 (106)	Full (1412)	Representative proteomes				UniProt (4670)	NCBI (4642)	Meta (21)
	Seed (106)	Full (1412)	RP15 (475)	RP35 (762)	RP55 (1148)	RP75 (1321)	UniProt (4670)	NCBI (4642)	Meta (21)
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PP/heatmap	₁	View

¹Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: available, not generated, — not available.

Format an alignment

	Seed (106)	Full (1412)	Representative proteomes				UniProt (4670)	NCBI (4642)	Meta (21)
	Seed (106)	Full (1412)	RP15 (475)	RP35 (762)	RP55 (1148)	RP75 (1321)	UniProt (4670)	NCBI (4642)	Meta (21)
Alignment:
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Order:	Tree Alphabetical
Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

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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 (106)	Full (1412)	Representative proteomes				UniProt (4670)	NCBI (4642)	Meta (21)
	Seed (106)	Full (1412)	RP15 (475)	RP35 (762)	RP55 (1148)	RP75 (1321)	UniProt (4670)	NCBI (4642)	Meta (21)
Raw Stockholm	Download	Download	Download	Download	Download	Download	Download	Download	Download
Gzipped	Download	Download	Download	Download	Download	Download	Download	Download	Download

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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Curation and family details

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Curation

Seed source:

Prosite

Previous IDs:

none

Type:

Domain

Sequence Ontology:

SO:0000417

Author:

Finn RD

, Griffiths-Jones SR

Number in seed:

106

Number in full:

1412

Average length of the domain:

67.20 aa

Average identity of full alignment:

46 %

Average coverage of the sequence by the domain:

15.74 %

HMM information

HMM build commands:

build method: hmmbuild -o /dev/null HMM SEED

search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq

Model details:

Parameter	Sequence	Domain
Gathering cut-off	25.7	25.7
Trusted cut-off	26.3	27.0
Noise cut-off	25.5	25.0

Model length:

67

Family (HMM) version:

15

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Species distribution

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Interactive tree

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Interactions

There are 2 interactions for this family. More...

ATP-gua_Ptrans ATP-gua_Ptrans

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 140 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.

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Family: ATP-gua_PtransN (PF02807)

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Summary: ATP:guanido phosphotransferase, N-terminal domain

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ATP:guanido phosphotransferase family Edit Wikipedia article

References

ATP:guanido phosphotransferase, N-terminal domain Provide feedback

Literature references

External database links

InterPro entry IPR022413

Gene Ontology

Domain organisation

Alignments

Alignment types

Viewing

Reformatting

Downloading

View options

Format an alignment

Download options

HMM logo

Trees

Curation and family details

Curation

HMM information

Species distribution

Sunburst controls

Weight segments by...

Change the size of the sunburst

Colour assignments

Selections

Currently selected:

How the sunburst is generated

Colouring and labels

Anomalies in the taxonomy tree

Missing taxonomic levels

Unmapped species names

Sub-species

Too many species/sequences

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Annotation

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Species trees

Interactive tree

Interactions

Structures

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