0  structures 355  species 0  interactions 744  sequences 6  architectures

Family: H_PPase (PF03030)

Summary

Inorganic H+ pyrophosphatase Add an annotation

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

  1. Drozdowicz YM, Rea PA; , Trends Plant Sci 2001;6:206-211.: Vacuolar H(+) pyrophosphatases: from the evolutionary backwaters into the mainstream. PUBMED:11335173


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 () 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

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Domain organisation

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Alignments

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The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

Pfam alignments:
Full length sequences

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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 View help on the curation process

Seed source: Pfam-B_1050 (release 6.4)
Previous IDs: none
Type: Family
Author: Griffiths-Jones SR
Number in seed: 140
Number in full: 744
Average length of the domain: 588.10 aa
Average identity of full alignment: 44 %
Average coverage of the sequence by the domain: 93.26 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.2 22.2
Trusted cut-off 22.4 22.4
Noise cut-off 20.8 20.4
Model length: 684
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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