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
tpiATriosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (226 aa)    
Predicted Functional Partners:
pgk
HAMAP: Phosphoglycerate kinase; KEGG: mth:MTH1042 phosphoglycerate kinase; PFAM: Phosphoglycerate kinase; Belongs to the phosphoglycerate kinase family.
 
 
 0.999
eno
Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family.
  
 
 0.998
gap
KEGG: mth:MTH1009 glyceraldehyde-3-phosphate dehydrogenase; PFAM: Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain; Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain; TIGRFAM: Glyceraldehyde-3-phosphate dehydrogenase, type II; HAMAP: Glyceraldehyde-3-phosphate dehydrogenase; SMART: Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain.
 
 0.998
gap-2
KEGG: mmg:MTBMA_c13910 glyceraldehyde 3-phosphate dehydrogenase; PFAM: Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain; Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain; TIGRFAM: Glyceraldehyde-3-phosphate dehydrogenase, type II; HAMAP: Glyceraldehyde-3-phosphate dehydrogenase; SMART: Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain.
 
 0.998
aroA-2
Phospho-2-dehydro-3-deoxyheptonate aldolase; Catalyzes a transaldol reaction between 6-deoxy-5- ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7- dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.
 
 
 0.964
ADZ08367.1
KEGG: mru:mru_2213 fuculose 1-phosphate aldolase FucA; PFAM: Class II aldolase/adducin, N-terminal.
  
 
 0.953
rpl4
50S ribosomal protein L4P; Forms part of the polypeptide exit tunnel.
 
  
 0.952
fbp
Protein of unknown function DUF100; Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3- phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).
 
  
 0.951
deoC
Deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate; Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
  
 0.905
carS
UPF0290 protein; Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn- glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1- phosphate (DGGGP) and CTP. This reaction is the third ether-bond- formation step in the biosynthesis of archaeal membrane lipids.
 
   
 0.823
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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