STRINGSTRING
adk protein (Gloeobacter violaceus) - STRING interaction network
"adk" - Adenylate kinase in Gloeobacter violaceus
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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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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adkAdenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (220 aa)    
Predicted Functional Partners:
gll3495
Pyruvate kinase (605 aa)
 
 
  0.958
atpA
ATP synthase F0F1 subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (513 aa)
   
 
  0.953
gll3323
Pyruvate kinase (473 aa)
 
 
  0.952
secY
Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (433 aa)
   
   
  0.946
glr4315
ATP synthase F0F1 subunit gamma; 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 (314 aa)
     
 
  0.945
pnp
Polynucleotide phosphorylase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3’- to 5’-direction (713 aa)
     
 
  0.941
apt
Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis (171 aa)
   
 
  0.938
gll2570
ATP synthase F0F1 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 (478 aa)
     
 
  0.938
ndk
Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (149 aa)
   
  0.930
gll2908
ATP synthase F0F1 subunit B’; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 proton translocation (174 aa)
     
 
  0.930
Your Current Organism:
Gloeobacter violaceus
NCBI taxonomy Id: 251221
Other names: G. violaceus, G. violaceus PCC 7421, Gloeobacter, Gloeobacter violaceus, Gloeobacter violaceus ATCC 29082, Gloeobacter violaceus PCC 7421, Gloeobacter violaceus str. PCC 7421, Gloeobacter violaceus strain PCC 7421, Gloeobacterales, Gloeobacterales Cavalier-Smith 2002, Gloeobacteria, Gloeobacteria Cavalier-Smith 2002
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