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
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[Homology]
Score
ACU95947.1Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Thiamine pyrophosphate enzyme, central domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. (620 aa)    
Predicted Functional Partners:
ACU95948.1
PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit.
 0.999
ilvC
Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
 
 
 0.994
ACU95955.1
PFAM: Isocitrate/isopropylmalate dehydrogenase.
 0.957
ACU97992.1
Tartrate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase; TIGRFAM: tartrate dehydrogenase.
 
 0.945
ilvA
L-threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
 
 0.937
ACU98157.1
L-threonine ammonia-lyase; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine dehydratase, medium form.
  
 0.935
ACU95414.1
2-oxoacid:ferredoxin oxidoreductase, alpha subunit; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-binding domain.
  
 
 0.933
ACU95958.1
2-isopropylmalate synthase; PFAM: LeuA allosteric (dimerisation) domain; HMGL-like; TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
 
 0.912
ilvD
PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
  
 0.911
ACU95413.1
2-oxoacid:ferredoxin oxidoreductase, beta subunit; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain.
  
 
 0.908
Your Current Organism:
Saccharomonospora viridis
NCBI taxonomy Id: 471857
Other names: S. viridis DSM 43017, Saccharomonospora viridis ATCC 15386, Saccharomonospora viridis DSM 43017, Saccharomonospora viridis NCIB 9602, Saccharomonospora viridis NRRL B-3044, Saccharomonospora viridis str. DSM 43017, Saccharomonospora viridis strain DSM 43017
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