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298  structures 6486  species 0  interactions 10593  sequences 82  architectures

Family: Pyrophosphatase (PF00719)

Summary: Inorganic pyrophosphatase

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Inorganic pyrophosphatase". More...

Inorganic pyrophosphatase Edit Wikipedia article

Pyrophosphatase (or inorganic pyrophosphatase) is a biochemical enzyme that converts one molecule of pyrophosphate to two phosphate ions. This highly exergonic reaction (about -34KJ change in free energy) can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion, as in Lipid synthesis and other biochemical transformations.

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.

Inorganic pyrophosphatase Provide feedback

No Pfam abstract.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR008162

Inorganic pyrophosphatase ( EC ) (PPase) [ PUBMED:2160278 , PUBMED:1323891 ] is the enzyme responsible for the hydrolysis of pyrophosphate (PPi) which is formed principally as the product of the many biosynthetic reactions that utilise ATP. All known PPases require the presence of divalent metal cations, with magnesium conferring the highest activity. Among other residues, a lysine has been postulated to be part of or close to the active site. PPases have been sequenced from bacteria such as Escherichia coli (homohexamer), Bacillus PS3 (Thermophilic bacterium PS-3) and Thermus thermophilus, from the archaebacteria Thermoplasma acidophilum, from fungi (homodimer), from a plant, and from bovine retina. In yeast, a mitochondrial isoform of PPase has been characterised which seems to be involved in energy production and whose activity is stimulated by uncouplers of ATP synthesis.

The sequences of PPases share some regions of similarities, among which is a region that contains three conserved aspartates that are involved in the binding of cations.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB 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
(498)
Full
(10593)
Representative proteomes UniProt
(35238)
RP15
(1626)
RP35
(4818)
RP55
(9865)
RP75
(16278)
Jalview View  View  View  View  View  View  View 
HTML View             
PP/heatmap 1            

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

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(498)
Full
(10593)
Representative proteomes UniProt
(35238)
RP15
(1626)
RP35
(4818)
RP55
(9865)
RP75
(16278)
Alignment:
Format:
Order:
Sequence:
Gaps:
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
(498)
Full
(10593)
Representative proteomes UniProt
(35238)
RP15
(1626)
RP35
(4818)
RP55
(9865)
RP75
(16278)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped 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.

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 View help on the curation process

Seed source: Pfam-B_613 (release 2.1)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 498
Number in full: 10593
Average length of the domain: 157.3 aa
Average identity of full alignment: 37 %
Average coverage of the sequence by the domain: 70.36 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.5 23.5
Trusted cut-off 23.6 23.6
Noise cut-off 23.4 23.4
Model length: 160
Family (HMM) version: 22
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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 Pyrophosphatase domain has been found. There are 298 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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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044V8B1 View 3D Structure Click here
A0A077ZKY5 View 3D Structure Click here
A0A0D2E0D3 View 3D Structure Click here
A0A0D2H6Q9 View 3D Structure Click here
A0A0G2JUD2 View 3D Structure Click here
A0A0H3GLK2 View 3D Structure Click here
A0A0H3GY84 View 3D Structure Click here
A0A0H5S079 View 3D Structure Click here
A0A0K0ENU9 View 3D Structure Click here
A0A0N4ULW0 View 3D Structure Click here
A0A0R0EZ04 View 3D Structure Click here
A0A0R0EZT3 View 3D Structure Click here
A0A0R0EZU8 View 3D Structure Click here
A0A0R0FVN7 View 3D Structure Click here
A0A0R0GZH8 View 3D Structure Click here
A0A0R0HPA5 View 3D Structure Click here
A0A0R0KVT1 View 3D Structure Click here
A0A0R4IMM5 View 3D Structure Click here
A0A0R4IRJ2 View 3D Structure Click here
A0A175W3S0 View 3D Structure Click here
A0A175WHD3 View 3D Structure Click here
A0A1C1CJX0 View 3D Structure Click here
A0A1D6GQZ9 View 3D Structure Click here
A0A1D6HHJ7 View 3D Structure Click here
A0A1D6LHK3 View 3D Structure Click here
A0A1D6Q7Z8 View 3D Structure Click here
A0A3P7ETR2 View 3D Structure Click here
A0A3Q0KVG2 View 3D Structure Click here
A2X8Q3 View 3D Structure Click here
A4HRX7 View 3D Structure Click here
A4HUT3 View 3D Structure Click here
B4FCR7 View 3D Structure Click here
B4FRR1 View 3D Structure Click here
B6TB84 View 3D Structure Click here
B7F8Y9 View 3D Structure Click here
B7ZD39 View 3D Structure Click here
C0H477 View 3D Structure Click here
C0NAJ6 View 3D Structure Click here
C1GQ62 View 3D Structure Click here
C6SYN5 View 3D Structure Click here