TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*3.A.10.1.1









H+-translocating vacuolar (tonoplast) pyrophosphatase of 770 aas, AVP1. 87% identical to the ortholog in rye (Secale cereale), found in the plasma membrane with 762 aas and 14 TMSs, ScHP1 (Wang et al. 2016). t contributes to the trans-tonoplast (from cytosol to vacuole lumen) H+-electrochemical potential difference and establishes a proton gradient of similar and often greater magnitude than the H+-ATPase in the same membrane (Kim et al. 1994). It also facilitates auxin transport by modulating the apoplastic pH, and it regulates auxin-mediated developmental processes (Li et al. 2005). It confers tolerance to NaCl and to drought by increasing ion retention (Gaxiola et al. 2001). H+-pyrophosphatases are major determinants of plant tolerance to amine fungicides (Hernández et al. 2016).

Eukaryota
Viridiplantae
V-PPase of Arabidopsis thaliana
*3.A.10.1.2









H+-translocating acidocalcisome pyrophosphatase

Eukaryota
Viridiplantae
V-PPase of Chlamydomonas reinhardtii
*3.A.10.1.3









Na+-translocating PPase (Malinen et al., 2007)
Bacteria
Firmicutes
Na-PPase of Moorella thermoacetica (Q2RIS7)
*3.A.10.1.4









Na+-translocating PPase (Malinen et al., 2007).  The 3-d resting state structure has been solved to 2.6 Å (Kellosalo et al. 2012).  The structure shows that the hydrolytic center is 20 Å above the membrane, coupled to the gate formed by the conserved Asp(243), Glu(246) and Lys(707) by an unusual "coupling funnel" of six α-helices. Helix 12 may slide down upon substrate binding to open the gate by a simple binding-change mechanism. Below the gate, four helices form the exit channel. Superimposing helices 3 to 6, 9 to 12, and 13 to 16 suggests that this PPases arose by gene triplication (Kellosalo et al. 2012).

Bacteria
Thermotogae
Na+-PPase of Thermatoga maritima (Q9S5X0)
*3.A.10.1.5









Na+-transporting, K+-dependent pyrophosphatase (Luoto et al., 2011).

Bacteria
Firmicutes
Na+-pyrophosphatase of Anaerostipes caccae (B0M926)
*3.A.10.1.6









Na+-transporting, K+-dependent pyrophosphatase (Luoto et al., 2011).

Bacteria
Bacteroidetes/Chlorobi group
Na+-pyrophosphatase of Chloronbium limicola (B3ECG6)
*3.A.10.1.7









K+-activated, H+-transporting pyrophosphatase, H+-PPase (Huang et al. 2013).  Trp-602 is a crucial residue that may stabilize the structure of the catalytic region (Chen et al. 2014).

Bacteria
Firmicutes
H+-PPase of Chlostridium tetani (Q898Q9)
*3.A.10.1.8









Vacuolar H+-PPase. 3-d structure known at 2.3 Å resolution (Charles et al., 2011; Lin et al. 2012).  Each  subunit consists of an integral membrane domain formed by 16 transmembrane helices.  imidodiphosphate is bound in the cytosolic surface of each subunit and trapped by numerous charged residues and five Mg2+ ions. A proton translocation pathway is formed by six core transmembrane helices. Proton pumping is initialized by PPi hydrolysis, and H+ is then transported into the vacuolar lumen through a pathway consisting of Arg242, Asp294, Lys742 and Glu301 (Lin et al. 2012).  Substrate binding induces changes in domain interactions (Hsu et al. 2015).

Eukaryota
Viridiplantae
H+-PPase of Vigna radiata (P21616)
*3.A.10.1.9









Vacuolar proton-translocating pyrophosphatase (Meng et al. 2011).

Eukaryota
Viridiplantae
Proton-PPase of Dunaliella viridis
*3.A.10.1.10









The K -stimulated H ,Na -PPase. Transports both Na  and H  noncompetitively in a single catalytic cycle (Luoto et al. 2013).

Bacteria
Bacteroidetes/Chlorobi group
H+,Na+-PPase of Bacteroides vulgatus (A6L2M4) 
*3.A.10.1.11









The K+-stimulated H+, Na+-PPase.  Transports both Na+ and H+ noncompetitively in a single catalytic cycle (Luoto et al., 2013a, b).

Bacteria
Bacteroidetes/Chlorobi group
H+, Na+-PPase of Prevotella oralis (E7RS29)
*3.A.10.1.12









The K+-stimulated H+, Na+-PPase. Transports both Na+ and H+ noncompetitively in a single catalytic cycle (Luoto et al., 2013a, b).

Bacteria
Chlamydiae/Verrucomicrobia group
H+, Na+-PPase of Verucomicrobiae bacterium (B5JQT8)
*3.A.10.1.13









The K+-stimulated H , Na +-PPase.  Transports both Na + and H + noncompetitively in a single catalytic cycle (Luoto et al., 2013a, b).

Bacteria
Firmicutes
The K -stimulated H , Na -PPase of Clostridium leptum
*3.A.10.1.14









K+-stimulated Na+-PPase 

Archaea
Euryarchaeota
K+-stimulated PPase of Methanosarcina mazei (Q8PYZ8)
*3.A.10.1.15









K+-insensitive pyrophosphatase-energized proton pump of 665 aas (Baltscheffsky and Persson 2014).

Archaea
Korarchaeota
PPase of Korarchaeum cryptofilum
*3.A.10.1.16









Vacuolar H+-pyrophosphatase of 771 aas, Ovp1.  Expression increases cold tolerance in rice (Zhang et al. 2011).  Rice also have a similar paralogue, Ovp2, of 767 aas (P93410).  It is 88% identical to Ovp1.  The corn (Zea mays) orthologue of 766 aas and 16 TMSs (97% identical to the rice protein), Vpp1, is up-regulated in shoots and roots of maize seedlings under dehydration, cold and high salt stresses, suggesting a role in abiotic stress tolerance (Yue et al. 2008).

Eukaryota
Viridiplantae
Ovp1 of Oriza sativa
*3.A.10.1.17









H+-transporting pyrophosphatase of 816 aas (Drozdowicz et al. 2003). It is inhibited by 5-10 μM aminomethylenediphosphonate (AMDP) which also inhibits trypomastigotes and parasite growth (Drozdowicz et al. 2003).

Eukaryota
Apicomplexa
H+-transporting pyrophosphatase of Toxoplasma gondii
*3.A.10.2.1









H+-translocating pyrophosphatase (PPiase)/synthase.  It has two distinct roles depending on its location, acting as a PPi hydrolyzing intracellular proton pump in acidocalcisomes but as a PPi synthetase in the chromatophore membranes (Seufferheld et al. 2004).

Bacteria
Proteobacteria
H+-PPase of Rhodospirillum rubrum (O68460)
*3.A.10.2.2









H+-translocating pyrophosphatase. This protein has a basic 16 TMS topology with several large cytoplasmic loops containing functional motifs as well as one or two C-terminal TMS(s) (Mimura et al., 2004).  Residues involved in energy coupling and proton transport have been identified (Hirono et al. 2007).

Bacteria
Actinobacteria
H+-PPase of Streptomyces coelicolor (Q6BCL0)
*3.A.10.2.3









Vacuolar Ca2+-hypersenstive, K+-insensitive, H+ -translocating, inorganic pyrophosphatase, AVP2 (Drozdowicz et al., 2000)
Eukaryota
Viridiplantae
AVP2 of Arabidopsis thaliana (Q56ZN6)
*3.A.10.2.4









Na+ -translocating PPase (Malinen et al., 2007)
Archaea
Euryarchaeota
Na+ -PPase of Methanosarcina mazei (Q8PYZ7)
*3.A.10.3.1









H+-translocating pyrophosphatase
Archaea
Crenarchaeota
H+-PPase of Pyrobaculum aerophilum
*3.A.10.3.2









Membrane-bound sodium- and potassium-regulated, proton-translocating pyrophosphatase of 806 aas. One report claims it transports only H+, not Na+ and that Na+ inhibits by competing with Mg2+ (Luoto et al. 2015), although a previous report claimed that it transports Na+ under normal physiological conditions, but protons if the Na+ concentration is low (Luoto et al. 2013).

Bacteria
Bacteroidetes/Chlorobi group
Na+/H+-PPase of Chlorobium limicola
*3.A.10.3.3









Electrogenic H+-translocating Mg2+-pyrophosphatase, HhpA of 867 aas.  Inhibited by Na+ and regulated by K+ as well (Luoto et al. 2015).

Bacteria
Actinobacteria
P2ase of Cellulomonas fimi
*3.A.10.3.4









H+ or Na+-translocating pyrophosphatase of 797 aas, HppA (Luoto et al. 2015).

Bacteria
Bacteroidetes/Chlorobi group
Pyrophosphatase of Azobacteroides pseudotrichonymphae genomovar. CFP2
*3.A.10.3.5









H+-translocating pyrophosphatase of 836 aas, HppA (Luoto et al. 2015)

Bacteria
Proteobacteria
P2ase of Accumulibacter phosphatis