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
Pmob_0123PFAM: UDP-N-acetylglucosamine 2-epimerase; KEGG: cha:CHAB381_1479 UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family. (367 aa)    
Predicted Functional Partners:
Pmob_0961
TIGRFAM: nucleotide sugar dehydrogenase; PFAM: UDP-glucose/GDP-mannose dehydrogenase; 6-phosphogluconate dehydrogenase NAD-binding; UDP-glucose/GDP-mannose dehydrogenase dimerisation; UDP-glucose/GDP-mannose dehydrogenase; KEGG: tpt:Tpet_0335 UDP-glucose 6-dehydrogenase; Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
 
 
 0.986
Pmob_1283
Polysaccharide biosynthesis protein CapD; PFAM: NAD-dependent epimerase/dehydratase; 3-beta hydroxysteroid dehydrogenase/isomerase; polysaccharide biosynthesis protein CapD; Male sterility domain; Polysaccharide biosynthesis domain protein; KEGG: drm:Dred_3033 polysaccharide biosynthesis protein CapD.
  
 
 0.916
glmU
UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain.
    
 0.912
murA
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily.
  
 
 0.906
Pmob_1284
PFAM: UDP-N-acetylglucosamine 2-epimerase; KEGG: bfs:BF1910 putative LPS biosynthesis related epimerase.
  
  
 
0.904
Pmob_1294
PFAM: UDP-N-acetylglucosamine 2-epimerase; KEGG: cha:CHAB381_1479 UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
  
  
 
0.900
Pmob_1662
PFAM: glycosyl transferase family 4; KEGG: fno:Fnod_0247 glycosyl transferase family 4.
 
  
 0.498
Pmob_0939
TIGRFAM: dTDP-glucose 4,6-dehydratase; PFAM: NAD-dependent epimerase/dehydratase; 3-beta hydroxysteroid dehydrogenase/isomerase; polysaccharide biosynthesis protein CapD; dTDP-4-dehydrorhamnose reductase; Male sterility domain; KEGG: tme:Tmel_1072 dTDP-glucose 4,6-dehydratase; Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.
  
  
 0.496
Pmob_0937
PFAM: DegT/DnrJ/EryC1/StrS aminotransferase; KEGG: bpu:BPUM_3223 aminotransferase; Belongs to the DegT/DnrJ/EryC1 family.
  
  
 0.438
Pmob_0960
PFAM: DegT/DnrJ/EryC1/StrS aminotransferase; aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: fno:Fnod_0174 DegT/DnrJ/EryC1/StrS aminotransferase; Belongs to the DegT/DnrJ/EryC1 family.
  
  
 0.438
Your Current Organism:
Petrotoga mobilis
NCBI taxonomy Id: 403833
Other names: P. mobilis SJ95, Petrotoga mobilis DSM 10674, Petrotoga mobilis SJ95, Petrotoga mobilis str. SJ95, Petrotoga mobilis strain SJ95
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.