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TCID	Name	Domain	Kingdom/Phylum	Protein(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). As expected, a pmf can be used via AVP1 to make pyrophosphate (Scholz-Starke et al. 2019).	Eukaryota	Viridiplantae, Streptophyta	V-PPase of Arabidopsis thaliana
3.A.10.1.2	H⁺-translocating acidocalcisome pyrophosphatase	Eukaryota	Viridiplantae, Chlorophyta	V-PPase of Chlamydomonas reinhardtii
3.A.10.1.3	Na⁺-translocating PPase (Malinen et al., 2007)	Bacteria	Bacillota	Na-PPase of Moorella thermoacetica (Q2RIS7)
3.A.10.1.4	Na⁺-translocating K⁺-stimulated PPase, HppA, of 726 aas and 16 TMSs (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	Thermotogota	Na⁺-PPase of Thermatoga maritima (Q9S5X0)
3.A.10.1.5	Na⁺-transporting, K⁺-dependent pyrophosphatase (Luoto et al., 2011).	Bacteria	Bacillota	Na⁺-pyrophosphatase of Anaerostipes caccae (B0M926)
3.A.10.1.6	Na⁺-transporting, K⁺-dependent pyrophosphatase (Luoto et al., 2011).	Bacteria	Chlorobiota	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	Bacillota	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 PP_i 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, Streptophyta	H⁺-PPase of Vigna radiata (P21616)
3.A.10.1.9	Vacuolar proton-translocating pyrophosphatase (Meng et al. 2011).	Eukaryota	Viridiplantae, Chlorophyta	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	Bacteroidota	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	Bacteroidota	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	Verrucomicrobiota	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	Bacillota	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	Candidatus 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, Streptophyta	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.10.1.18	Proton (H⁺) translocating pyrophosphatase in the alveolar sac, of 746 aas and ~16 TMSs. It is a homodimer involved in organellar acidification (Folgueira et al. 2021).	Eukaryota	Ciliophora	H⁺-PPase of Philasterides dicentrarchi
3.A.10.1.19	Vacuolar H⁺ importing pyrophosphatase, VP1, of 717 aas and 16 TMSs in an apparent 5 + 6 + 5 TMS arrangement.	Eukaryota	Apicomplexa	H⁺-pumping diphosphatase, VP1, of Plasmodium falciparum
3.A.10.1.20	Sodium- and/or proton-translocating pyrophosphatase of 719 aas and 16 TMSs in a 5 + 6 + 5 TMS arrangement.	Archaea	Asgard	ion transporting pyrophosphatase of an Asgard group archaeon
3.A.10.1.21	Pyrophosphate-energized vacuolar membrane proton pump 1 (BnVP1) of 763 aas and about 15 - 17 TMSs., possibly in a 5 + 6 + 5 TMS arrangement. Plants have developed defense mechanisms against cadmium (Cd) stress, with vacuolar compartmentalization of Cd²⁺ being a crucial process in Cd detoxification. The transport of Cd into vacuoles by these cation / H⁺ antiporters is powered by the pH gradient created by proton pumps (Zhu et al. 2024). BnVP1 expression was significantly higher in ramie roots than in shoots. Cd treatments markedly induced BnVP1 expression in both roots and leaves of ramie seedlings, with a more pronounced effect in roots. Additionally, BnVP1 expression was significantly upregulated by the plant hormone methyl jasmonate (MeJA). Heterologous expression of BnVP1 in transgenic Arabidopsis significantly enhanced V-PPase activity in the roots. The growth performance, root elongation, and total chlorophyll content of transgenic plants with high tonoplast H⁺-PPase (V-PPase) activity were superior to those of wild-type plants. Overexpression of BnVP1 reduced membrane lipid peroxidation and ion leakage, and significantly increased Cd accumulation in the roots of transgenic Arabidopsis seedlings (Zhu et al. 2024). BnVP1 confers cadmium tolerance in Arabidopsis thaliana.	Eukaryota	Viridiplantae, Streptophyta	BnVP1 of Boehmeria nivea
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	Pseudomonadota	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). H⁺-PPase may be present as an oligomer made up of at least two or three sets of dimers (Mimura et al. 2005).	Bacteria	Actinomycetota	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, Streptophyta	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.10.2.5	H⁺-Pyrophosphatase of 810 aas and ~17 TMSs. It is present in intracellular vacuoles and functions in vacuolar acidification and homeostasis (Folgueira et al. 2021).	Eukaryota	Ciliophora	H+-pyrophosphatase of Philasterides dicentrarchi
3.A.10.2.6	Vacuolar Ca²⁺-dependent H⁺ pumping pyrophosphatase, PPase or VP2, of 1057 aas and ~ 18 TMSs in a 2 + 1 + 2 + 5 + 10 TMS arrangement (Wunderlich 2022).	Eukaryota	Apicomplexa	PPase, VP2, of Plasmodium falciparum
3.A.10.3.1	H⁺-translocating pyrophosphatase	Archaea	Thermoproteota	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	Chlorobiota	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	Actinomycetota	P2ase of Cellulomonas fimi
3.A.10.3.4	H⁺ or Na⁺-translocating pyrophosphatase of 797 aas, HppA (Luoto et al. 2015).	Bacteria	Bacteroidota	Pyrophosphatase of Azobacteroides pseudotrichonymphae genomovar. CFP2
3.A.10.3.5	H⁺-translocating pyrophosphatase of 836 aas, HppA (Luoto et al. 2015)	Bacteria	Pseudomonadota	P₂ase of Accumulibacter phosphatis