Summary: Polyphosphate kinase middle domain
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This is the Wikipedia entry entitled "Polyphosphate kinase". More...
Polyphosphate kinase Edit Wikipedia article
| polyphosphate kinase | |||||||||
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| Identifiers | |||||||||
| EC number | 2.7.4.1 | ||||||||
| CAS number | 9026-44-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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| Polyphosphate kinase | |||||||||
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| Identifiers | |||||||||
| Symbol | PP_kinase | ||||||||
| Pfam | PF02503 | ||||||||
| InterPro | IPR003414 | ||||||||
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In enzymology, a polyphosphate kinase (EC 2.7.4.1) is an enzyme that catalyzes the formation of polyphosphate from ATP, with chain lengths of up to a thousand or more orthophosphate molecules.[1]
- ATP + (phosphate)n
ADP + (phosphate)n+1
Thus, the two substrates of this enzyme are ATP and (phosphate)n, whereas its two products are ADP and (phosphate)n+1.
It is a membrane protein and goes through an intermediate stage during the reaction where it is autophosphorylated with a phosphate group covalently linked to a basic amino acid residue through an N-P bond.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:polyphosphate phosphotransferase. This enzyme is also called polyphosphoric acid kinase. This enzyme participates in oxidative phosphorylation.
[edit] Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1XDO, 1XDP, and 2O8R.
[edit] References
- ^ Brown MR, Kornberg A (June 2008). "The long and short of it - polyphosphate, PPK and bacterial survival". Trends Biochem. Sci. 33 (6): 284–90. doi:10.1016/j.tibs.2008.04.005. PMID 18487048.
[edit] Further reading
- Hoffmann-Ostenhof O, Kenedy J, Keck K, Gabriel O, Schonfellinger HW (1954). "A new transphosphorylase from yeast.". Biochim. Biophys. Acta. 14 (2): 285. PMID 13172250.
- Kornberg A, Kornberg SR, Simms ES (1956). "Metaphosphate synthesis by an enzyme from Escherichia coli". Biochim. Biophys. Acta. 20 (1): 215–27. doi:10.1016/0006-3002(56)90280-3. PMID 13315368.
- Muhammed A (1961). "Studies on biosynthesis of polymetaphosphate by an enzyme from Corynebacterium xerosis". Biochim. Biophys. Acta 54: 121–132. doi:10.1016/0006-3002(61)90945-3. PMID 14476999.
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Polyphosphate kinase middle domain Provide feedback
Polyphosphate kinase (Ppk) catalyses the formation of polyphosphate from ATP, with chain lengths of up to a thousand or more orthophosphate molecules.
Literature references
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Geissdorfer W, Ratajczak A, Hillen W; , Appl Environ Microbiol 1998;64:896-901.: Transcription of ppk from Acinetobacter sp. strain ADP1, encoding a putative polyphosphate kinase, is induced by phosphate starvation. PUBMED:9501429 EPMC:9501429
External database links
| PANDIT: | PF02503 |
| Pseudofam: | PF02503 |
| SYSTERS: | PP_kinase |
This tab holds annotation information from the InterPro database.
InterPro entry IPR024953
Polyphosphate kinase (Ppk) catalyses the formation of polyphosphate from ATP, with chain lengths of up to a thousand or more orthophosphate molecules [PUBMED:9501429]. This entry represents the Ppk middle domain.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...
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 (173) |
Full (3692) |
Representative proteomes | NCBI (2965) |
Meta (1012) |
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| RP15 (208) |
RP35 (457) |
RP55 (598) |
RP75 (697) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
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 (173) |
Full (3692) |
Representative proteomes | NCBI (2965) |
Meta (1012) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (208) |
RP35 (457) |
RP55 (598) |
RP75 (697) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
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.
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: | Pfam-B_2701 (release 5.4) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Mian N, Bateman A |
| Number in seed: | 173 |
| Number in full: | 3692 |
| Average length of the domain: | 200.80 aa |
| Average identity of full alignment: | 31 % |
| Average coverage of the sequence by the domain: | 31.95 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 207 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
PP_kinaseStructures
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 PP_kinase domain has been found. There are 6 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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ADP + (phosphate)n+1
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence