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AT2G25610 AT2G25610 PB PB VHA-C3 VHA-C3 AT5G08690 AT5G08690 ATPA ATPA ATP1 ATP1 ATPC2 ATPC2 ATPC1 ATPC1 PPa1 PPa1 AT4G32530 AT4G32530 ATP3 ATP3
"PPa1" - Pyrophosphorylase 1 in Arabidopsis thaliana
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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PPa1Pyrophosphorylase 1; Catalyzes the irreversible hydrolysis of pyrophosphate (PPi) to phosphate. The MgPPi(2-) complex binds to the enzyme only after a free Mg(2+) ion has bound (Ref.9). No activity with glycerol-3-phosphate, glucose-6-phosphate, p-nitrophenylphosphate, ADP, NADP(+), NAD(+),NADH, NADPH or phosphoribosyl pyrophosphate as substrates (Ref.9). Controls the equilibrium of gluconeogenic reactions in the heterotrophic growth phase of early seedling establishment. Determinates the rate of cytosolic glycolysis, providing carbon for seed storage lipid accumulation (PubMed-22566496) (212 aa)    
Predicted Functional Partners:
ATP1
ATPase subunit 1; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to [...] (507 aa)
     
 
  0.943
ATPA
ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (507 aa)
     
 
  0.943
AT4G32530
ATPase, F0/V0 complex, subunit C protein (210 aa)
     
  0.938
AT2G25610
ATPase, F0/V0 complex, subunit C protein; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity) (178 aa)
     
  0.938
ATP3
ATP synthase subunit gamma; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk s [...] (325 aa)
     
 
  0.928
ATPC1
ATP synthase gamma chain 1; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex (373 aa)
     
 
  0.924
ATPC2
ATP synthase gamma chain 2; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex (386 aa)
     
 
  0.924
VHA-C3
Vacuolar-type H(+)-ATPase C3; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (164 aa)
     
  0.919
PB
ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits (498 aa)
     
 
  0.919
AT5G08690
ATP synthase subunit beta-2; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk [...] (556 aa)
     
 
  0.919
Your Current Organism:
Arabidopsis thaliana
NCBI taxonomy Id: 3702
Other names: A. thaliana, Arabidopsis thaliana, Arabidopsis thaliana (L.) Heynh., mouse-ear cress, thale cress, thale-cress
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