Summary: Inorganic H+ pyrophosphatase
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This is the Wikipedia entry entitled "Inorganic diphosphatase". More...
Inorganic diphosphatase Edit Wikipedia article
| inorganic diphosphatase | |||||||
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| Identifiers | |||||||
| EC number | 3.6.1.1 | ||||||
| CAS number | 9024-82-2 | ||||||
| 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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In enzymology, an inorganic diphosphatase (EC 3.6.1.1) is an enzyme that catalyzes the chemical reaction
- diphosphate + H2O
2 phosphate
Thus, the two substrates of this enzyme are diphosphate and H2O, whereas its product is phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is diphosphate phosphohydrolase. This enzyme participates in oxidative phosphorylation. It employs one cofactor, metal.
[edit] References
[edit] Further reading
- Bailey K and Webb EC (1944). "Purification and properties of yeast pyrophosphatase". Biochem. J. 38 (5): 394–398. PMC 1258115. PMID 16747821. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1258115.
- KUNITZ M (1952). "CRYSTALLINE INORGANIC PYROPHOSPHATASE ISOLATED FROM BAKER'S YEAST". J. Gen. Physiol. 35 (3): 423–50. DOI:10.1085/jgp.35.3.423. PMC 2147340. PMID 14898026. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2147340.
- Rafter GW (1960). "Pyrophosphate metabolism in liver mitochondria". J. Biol. Chem. 235: 2475–2477.
- Sarafian V, Kim Y, Poole RJ, Rea PA (March 1992). "Molecular cloning and sequence of cDNA encoding the pyrophosphate-energized vacuolar membrane proton pump of Arabidopsis thaliana". Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1775–9. DOI:10.1073/pnas.89.5.1775. PMC 48535. PMID 1311852. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=48535.
- Drozdowicz YM, Lu YP, Patel V, Fitz-Gibbon S, Miller JH, Rea PA (November 1999). "A thermostable vacuolar-type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum: implications for the origins of pyrophosphate-energized pumps". FEBS Lett. 460 (3): 505–12. DOI:10.1016/S0014-5793(99)01404-0. PMID 10556526.
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Inorganic H+ pyrophosphatase Provide feedback
The H+ pyrophosphatase is an transmembrane proton pump involved in establishing the H+ electrochemical potential difference between the vacuole lumen and the cell cytosol. Vacuolar-type H(+)-translocating inorganic pyrophosphatases have long been considered to be restricted to plants and to a few species of photo-trophic bacteria. However, in recent investigations, these pyrophosphatases have been found in organisms as disparate as thermophilic Archaea and parasitic protists [1].
Literature references
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Drozdowicz YM, Rea PA; , Trends Plant Sci 2001;6:206-211.: Vacuolar H(+) pyrophosphatases: from the evolutionary backwaters into the mainstream. PUBMED:11335173 EPMC:11335173
External database links
| PANDIT: | PF03030 |
| Pseudofam: | PF03030 |
| SYSTERS: | H_PPase |
| Transporter classification: | 3.A.10 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004131
Two types of proteins that hydrolyse inorganic pyrophosphate (PPi), very different in both amino acid sequence and structure, have been characterised to date: soluble and membrane-bound proton-pumping pyrophosphatases (sPPases and H(+)-PPases, respectively). sPPases are ubiquitous proteins that hydrolyse PPi to release heat, whereas H+-PPases, so far unidentified in animal and fungal cells, couple the energy of PPi hydrolysis to proton movement across biological membranes [PUBMED:12451180, PUBMED:10523139]. The latter type is represented by this group of proteins. H+-PPases (EC) are also called vacuolar-type inorganic pyrophosphatases (V-PPase) or pyrophosphate-energised vacuolar membrane proton pumps [PUBMED:11343697]. In plants, vacuoles contain two enzymes for acidifying the interior of the vacuole, the V-ATPase and the V-PPase (V is for vacuolar) [PUBMED:10523139].
Two distinct biochemical subclasses of H+-PPases have been characterised to date: K+-stimulated and K+-insensitive [PUBMED:12451180, PUBMED:11343697].
For additional information please see [PUBMED:1311852, PUBMED:10556526].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | membrane (GO:0016020) |
| Molecular function | inorganic diphosphatase activity (GO:0004427) |
| hydrogen-translocating pyrophosphatase activity (GO:0009678) | |
| Biological process | proton transport (GO:0015992) |
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...
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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 (139) |
Full (1540) |
Representative proteomes | NCBI (1460) |
Meta (5022) |
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| RP15 (268) |
RP35 (465) |
RP55 (553) |
RP75 (611) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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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 (139) |
Full (1540) |
Representative proteomes | NCBI (1460) |
Meta (5022) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (268) |
RP35 (465) |
RP55 (553) |
RP75 (611) |
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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_1050 (release 6.4) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Griffiths-Jones SR |
| Number in seed: | 139 |
| Number in full: | 1540 |
| Average length of the domain: | 626.60 aa |
| Average identity of full alignment: | 43 % |
| Average coverage of the sequence by the domain: | 93.38 % |
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: | 682 | ||||||||||||
| Family (HMM) version: | 11 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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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 H_PPase domain has been found. There are 2 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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2 phosphate
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence