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Mettu_3679 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_3679" - Vitamin B12-dependent ribonucleotide reductase in Methylobacter tundripaludum
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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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Mettu_3679Vitamin B12-dependent ribonucleotide reductase; Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen (716 aa)    
Predicted Functional Partners:
Mettu_3680
KEGG- ttu-TERTU_1636 ribonucleotide reductase, alpha subunit (254 aa)
   
  0.994
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 (143 aa)
     
 
  0.982
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
   
  0.975
dut
Deoxyuridine 5’-triphosphate nucleotidohydrolase; This enzyme is involved in nucleotide metabolism- it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family (154 aa)
   
 
  0.967
Mettu_1599
UPF0301 protein Mettu_1599; KEGG- mca-MCA2336 hypothetical protein; HAMAP- Protein of unknown function DUF179; PFAM- Protein of unknown function DUF179; Belongs to the UPF0301 (AlgH) family (187 aa)
     
  0.949
Mettu_1953
Beta sliding clamp; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3’-5’ exonuclease proofreading activity. The beta chain is required for initiation of replication as [...] (366 aa)
     
 
  0.904
tmk
Thymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (223 aa)
   
 
  0.879
atpD
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 (459 aa)
     
 
  0.874
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2’-deoxyuridine- 5’-monophosphate (dUMP) to 2’-deoxythymidine-5’-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis (277 aa)
   
   
  0.866
Mettu_3681
annotation not available (161 aa)
              0.845
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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