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

PANDIT:	PF02807
PROSITE:	PDOC00103
Pseudofam:	PF02807
SCOP:	1crk
SYSTERS:	ATP-gua_PtransN

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

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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

We make a range of alignments for each Pfam-A family:

seed: the curated alignment from which the HMM for the family is built
full: the alignment generated by searching the sequence database using the HMM
RP15/RP35/RP55/RP75: Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
NCBI: alignment generated by searching the NCBI sequence database using the family HMM
meta: alignment generated by searching the metagenomics sequence database using the family HMM

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Pfam viewer: an HTML-based viewer that uses DAS to retrieve alignment fragments on request

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You may find that large alignments cause problems for the viewers and the reformatting tool, so we also provide all alignments in Stockholm format. You can download either the plain text alignment, or a gzipped version of it.

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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 (91)	Full (1908)	Representative proteomes				NCBI (1509)	Meta (23)
	Seed (91)	Full (1908)	RP15 (158)	RP35 (187)	RP55 (276)	RP75 (380)	NCBI (1509)	Meta (23)
Jalview	View	View	View	View	View	View	View	View
HTML	View	View	View	View	View	View
PP/heatmap	₁	View	View	View	View	View
Pfam viewer	View	View

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

Key: available, not generated, — not available.

Format an alignment

	Seed (91)	Full (1908)	Representative proteomes				NCBI (1509)	Meta (23)
	Seed (91)	Full (1908)	RP15 (158)	RP35 (187)	RP55 (276)	RP75 (380)	NCBI (1509)	Meta (23)
Alignment:
Format:
Order:	Tree Alphabetical
Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

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 (91)	Full (1908)	Representative proteomes				NCBI (1509)	Meta (23)
	Seed (91)	Full (1908)	RP15 (158)	RP35 (187)	RP55 (276)	RP75 (380)	NCBI (1509)	Meta (23)
Raw Stockholm	Download	Download	Download	Download	Download	Download	Download	Download
Gzipped	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.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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Trees

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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

Author:

Finn RD, Griffiths-Jones SR

Number in seed:

91

Number in full:

1908

Average length of the domain:

67.60 aa

Average identity of full alignment:

62 %

Average coverage of the sequence by the domain:

24.46 %

HMM information

HMM build commands:

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

search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq

Model details:

Parameter	Sequence	Domain
Gathering cut-off	25.7	25.7
Trusted cut-off	25.7	26.1
Noise cut-off	25.6	25.5

Model length:

76

Family (HMM) version:

10

Download:

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Species distribution

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Unmapped species names

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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.

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Interactive tree

For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.

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Interactions

There is 1 interaction for this family. More...

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 104 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 seqence.

Loading structure mapping...

Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
Viroids	Unclassified sequence

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

External links

HMM logo

Trees

Curation and family details

Curation

HMM information

Species distribution

Sunburst controls

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Change the size of the sunburst

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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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Selected sequences

Species trees

Interactive tree

Interactions

Structures