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104  structures 2750  species 2  interactions 3578  sequences 21  architectures

Family: ATP-gua_Ptrans (PF00217)

Summary: ATP:guanido phosphotransferase, C-terminal catalytic domain

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This is the Wikipedia entry entitled "ATP:guanido phosphotransferase family". More...

ATP:guanido phosphotransferase family Edit Wikipedia article

ATP:guanido phosphotransferase catalytic domain
PDB 1sd0 EBI.jpg
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
PDB 1p50 EBI.jpg
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:

  • Smc74, a cercaria-specific enzyme from Schistosoma mansoni.[1]

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

  1. ^ 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. 
  2. ^ 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. 
  3. ^ 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. 
  4. ^ 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. 
  5. ^ 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, C-terminal catalytic domain Provide feedback

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.

Literature references

  1. 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

This tab holds annotation information from the InterPro database.

InterPro entry IPR022414

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.

Eukaryotic phosphagen kinases consist of a small, ~100-residue, alpha-helical N-terminal domain and a larger, 250+- residue, C-terminal alpha/beta saddle domain in which many key residues involved in catalysis are found. The N-terminal domain undergoes significant conformational movements during catalysis, closing down on the catalytic pocket. It is involved in dimer formation. Bacterial phosphagen kinases have the large C-terminal domain seen in eukaryotic phosphagen kinases but lack the N-terminal domain [PUBMED:17932618, PUBMED:18064398, PUBMED:18499493, PUBMED:20121101].

This entry represents the C-terminal catalytic domain of ATP:guanido phosphotransferase, which is comprised of a duplication where the common core consists of two beta-alpha-beta2-alpha repeats [PUBMED:8692275]. 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 [PUBMED:8692275].

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan GCS (CL0286), which has the following description:

This clan represents a superfamily of carboxylate-amine/ammonia ligases [1] that includes Gamma-Glutamylcysteine synthetase (gamma-GCS) and glutamine synthetase (GS). Gamma-Glutamylcysteine synthetase (gamma-GCS) catalyses the first step in the de novo biosynthesis of glutathione.

The clan contains the following 9 members:

Amidoligase_2 ATP-gua_Ptrans COOH-NH2_lig DUF2126 GCS GCS2 Gln-synt_C Glu_cys_ligase Pup_ligase

Alignments

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  Seed
(115)
Full
(3578)
Representative proteomes NCBI
(2666)
Meta
(91)
RP15
(243)
RP35
(305)
RP55
(418)
RP75
(545)
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  Seed
(115)
Full
(3578)
Representative proteomes NCBI
(2666)
Meta
(91)
RP15
(243)
RP35
(305)
RP55
(418)
RP75
(545)
Alignment:
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  Seed
(115)
Full
(3578)
Representative proteomes NCBI
(2666)
Meta
(91)
RP15
(243)
RP35
(305)
RP55
(418)
RP75
(545)
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

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.

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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.

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Seed source: Prosite
Previous IDs: none
Type: Domain
Author: Finn RD, Griffiths-Jones SR
Number in seed: 115
Number in full: 3578
Average length of the domain: 185.20 aa
Average identity of full alignment: 48 %
Average coverage of the sequence by the domain: 68.74 %

HMM information View help on HMM parameters

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 21.9 21.9
Trusted cut-off 23.1 23.0
Noise cut-off 21.8 21.4
Model length: 243
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Interactions

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

ATP-gua_PtransN 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_Ptrans 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.

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