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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
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[Homology]
Score
Ping_0789PFAM: NAD-dependent epimerase/dehydratase; short-chain dehydrogenase/reductase SDR; 3-beta hydroxysteroid dehydrogenase/isomerase; polysaccharide biosynthesis protein CapD; dTDP-4-dehydrorhamnose reductase; Male sterility C-terminal domain; Polysaccharide biosynthesis C-terminal domain protein; KEGG: vfi:VF0191 UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose 3,5-epimerase. (345 aa)    
Predicted Functional Partners:
Ping_0791
PFAM: UDP-N-acetylglucosamine 2-epimerase; KEGG: lic:LIC12139 UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
 
  
 0.965
Ping_0431
PFAM: UDP-N-acetylglucosamine 2-epimerase; KEGG: ypn:YPN_0099 UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
  
 
 0.936
Ping_0790
dTDP-4-dehydrorhamnose reductase; Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose; Belongs to the dTDP-4-dehydrorhamnose reductase family.
 
  
 0.923
Ping_3456
Nucleotide sugar epimerase/dehydratase; PFAM: NAD-dependent epimerase/dehydratase; short-chain dehydrogenase/reductase SDR; 3-beta hydroxysteroid dehydrogenase/isomerase; polysaccharide biosynthesis protein CapD; Male sterility C-terminal domain; KEGG: vvu:VV10775 predicted nucleoside-diphosphate sugar epimerase.
  
  
 
0.923
Ping_0792
PFAM: glycosyl transferase, group 1; KEGG: lic:LIC12138 colanic acid biosynthesis glycosyl-transferase.
 
  
 0.912
glmU
UDP-N-acetylglucosamine pyrophosphorylase / glucosamine-1-phosphate N-acetyltransferase; 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. In the C-terminal section; belongs to the t [...]
    
 0.912
Ping_0775
PFAM: DegT/DnrJ/EryC1/StrS aminotransferase; aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: vfi:VF0184 CDP-4-dehydro-6-deoxy-D-glucose 3-dehydratase; Belongs to the DegT/DnrJ/EryC1 family.
  
 0.831
Ping_0766
KEGG: pat:Patl_1792 mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; TIGRFAM: mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; PFAM: mannose-6-phosphate isomerase, type II; Nucleotidyl transferase; Cupin 2, conserved barrel domain protein.
  
  
 0.781
Ping_3457
PFAM: NAD-dependent epimerase/dehydratase; 3-beta hydroxysteroid dehydrogenase/isomerase; sugar transferase; polysaccharide biosynthesis protein CapD; dTDP-4-dehydrorhamnose reductase; Male sterility C-terminal domain; KEGG: pen:PSEEN1504 UDP-glucose 4-epimerase.
 
  
 0.772
Ping_0788
KEGG: vvy:VV0348 hypothetical protein.
       0.768
Your Current Organism:
Psychromonas ingrahamii
NCBI taxonomy Id: 357804
Other names: P. ingrahamii 37, Psychromonas ingrahamii 37, Psychromonas ingrahamii str. 37, Psychromonas ingrahamii strain 37, gas vacuolate str. 37
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