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
ALV26625.1tRNA threonylcarbamoyladenosine biosynthesis protein TsaE; Derived by automated computational analysis using gene prediction method: Protein Homology. (523 aa)    
Predicted Functional Partners:
ALV26532.1
tRNA threonylcarbamoyladenosine biosynthesis protein TsaB; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.982
ALV26623.1
Mannose-1-phosphate guanylyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.979
glmU
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.
    
 0.936
tsaD
tRNA threonylcarbamoyl adenosine modification protein TsaD; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family.
 
 
 0.920
ALV30047.1
Beta-glucosidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.920
ALV28877.1
Beta-hexosaminidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.920
ALV29884.1
PAS domain-containing sensor histidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.893
nnrD
NAD(P)H-hydrate epimerase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of bot [...]
  
 
 0.856
ALV25761.1
Translation factor Sua5; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
    
 0.692
ALV29557.1
PAS domain-containing sensor histidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.685
Your Current Organism:
Pannonibacter phragmitetus
NCBI taxonomy Id: 121719
Other names: Achromobacter group B, Achromobacter group E, Achromobacter sp. LMG 5410, Achromobacter sp. LMG 5411, Achromobacter sp. LMG 5430, Achromobacter sp. LMG 5431, DSM 14782, LMG 22736, LMG:22736, NCAIM B02025, NCTC 13350, P. phragmitetus, Pannonibacter phragmitetus Borsodi et al. 2003, alpha proteobacterium C6-19, alpha proteobacterium C6/17, alpha proteobacterium C6/8, strain C6/19
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