STRINGSTRING
STRING protein interaction network
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:
a 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 to 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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
mtnAMethylthioribose-1-phosphate isomerase; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). (346 aa)    
Predicted Functional Partners:
mtnP
Methylthioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates; Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
 
 
 0.979
Ppro_0283
PFAM: methylenetetrahydrofolate reductase; homocysteine S-methyltransferase; KEGG: gme:Gmet_0504 bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein.
   
  
 0.824
glnE
(Glutamate--ammonia-ligase) adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal tra [...]
       0.824
Ppro_1413
Methionine synthase (B12-dependent); PFAM: dihydropteroate synthase, DHPS; homocysteine S-methyltransferase; Methionine synthase, B12-binding module, cap domain protein; cobalamin B12-binding domain protein; KEGG: gme:Gmet_0549 homocysteine S-methyltransferase.
   
  
 0.822
Ppro_2543
L-fuculose 1-phosphate aldolase; PFAM: class II aldolase/adducin family protein; KEGG: pca:Pcar_3030 L-fuculose phosphate aldolase.
 
  
 0.793
Ppro_3241
PFAM: ribulose-phosphate 3-epimerase; KEGG: gsu:GSU3374 ribulose-phosphate 3-epimerase; Belongs to the ribulose-phosphate 3-epimerase family.
  
   0.731
ribH
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
  
    0.547
Ppro_0509
SMART: helicase c2; DEAD-like helicases-like; KEGG: gme:Gmet_3167 helicase C2.
       0.541
Ppro_0507
Two component transcriptional regulator, winged helix family; PFAM: response regulator receiver; transcriptional regulator domain protein; KEGG: gsu:GSU1879 DNA-binding response regulator.
       0.524
Ppro_0508
Histidine kinase; PFAM: ATP-binding region, ATPase domain protein domain protein; histidine kinase A domain protein domain protein; KEGG: gme:Gmet_1292 histidine kinase.
       0.524
Your Current Organism:
Pelobacter propionicus
NCBI taxonomy Id: 338966
Other names: P. propionicus DSM 2379, Pelobacter propionicus DSM 2379, Pelobacter propionicus str. DSM 2379, Pelobacter propionicus strain DSM 2379
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