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:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
Lbys_2276COGs: COG0059 Ketol-acid reductoisomerase; InterPro IPR013023:IPR013116:IPR000506; KEGG: sli:Slin_5912 ketol-acid reductoisomerase; PFAM: Acetohydroxy acid isomeroreductase catalytic domain-containing protein; acetohydroxy acid isomeroreductase; PRIAM: Ketol-acid reductoisomerase; SPTR: Ketol-acid reductoisomerase; TIGRFAM: ketol-acid reductoisomerase; PFAM: Acetohydroxy acid isomeroreductase, catalytic domain; TIGRFAM: ketol-acid reductoisomerase. (347 aa)    
Predicted Functional Partners:
Lbys_2274
Acetolactate synthase, large subunit, biosynthetic type; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterProIPR000399:IPR001917:IPR012846:IPR012001:IPR 012000:IPR011766; KEGG: dfe:Dfer_3681 acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; SPTR: Acetolactate synthase; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding doma [...]
 
 
 0.999
Lbys_2275
COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR004789:IPR002912:IPR019455; KEGG: dfe:Dfer_3680 acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein; SPTR: Acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit.
 
 
 0.999
ilvD
COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; InterPro IPR020558:IPR004404:IPR000581; KEGG: dfe:Dfer_3684 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; PRIAM: Dihydroxy-acid dehydratase; SPTR: Dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.996
leuC
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
  
 0.983
leuD
3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
 
  
 0.896
leuB
3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
  
  
 0.861
Lbys_3304
COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; InterPro IPR000581; KEGG: dfe:Dfer_4563 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; PRIAM: Dihydroxy-acid dehydratase; SPTR: Dihydroxy-acid dehydratase; PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
 
  
 0.777
Lbys_1543
Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR000583:IPR006982:IPR002932:IPR002489:IPR 017932; KEGG: dfe:Dfer_5479 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Glutamate synthase (Ferredoxin); PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II.
  
  
 0.763
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.
 
  
 0.757
Lbys_1908
COGs: COG0498 Threonine synthase; InterPro IPR000634:IPR004450:IPR001926; KEGG: dfe:Dfer_3806 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; PRIAM: Threonine synthase; SPTR: Threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase.
  
  
 0.705
Your Current Organism:
Leadbetterella byssophila
NCBI taxonomy Id: 649349
Other names: L. byssophila DSM 17132, Leadbetterella byssophila 4M15, Leadbetterella byssophila DSM 17132, Leadbetterella byssophila str. DSM 17132, Leadbetterella byssophila strain DSM 17132
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.