STRINGSTRING
Mettu_1923 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1923" - HAD-superfamily hydrolase, subfamily IA, variant 3 in Methylobacter tundripaludum
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Mettu_1923HAD-superfamily hydrolase, subfamily IA, variant 3 (218 aa)    
Predicted Functional Partners:
Mettu_1869
Inosine-5’-monophosphate dehydrogenase (488 aa)
       
  0.885
guaA
Glutamine amidotransferase ; Catalyzes the synthesis of GMP from XMP (528 aa)
   
 
    0.884
Mettu_1924
NUDIX hydrolase (182 aa)
   
 
    0.818
secY
Protein 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 (440 aa)
       
      0.713
Mettu_1664
ImGP synthase subunit HisH ; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of IGP and AICAR (214 aa)
       
      0.657
Mettu_1474
ImGP synthase subunit HisH ; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of IGP and AICAR (221 aa)
       
      0.657
Mettu_2386
33 kDa chaperonin ; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress (289 aa)
   
 
    0.609
Mettu_2277
FAD linked oxidase domain protein (1224 aa)
       
    0.594
nadD
Nicotinate mononucleotide adenylyltransferase ; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (210 aa)
   
   
    0.587
purA
IMP--aspartate ligase ; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (430 aa)
   
    0.580
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
Server load: medium (46%) [HD]