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
ilvEBranched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (290 aa)    
Predicted Functional Partners:
ilvD
COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; HAMAP: Dihydroxy-acid dehydratase; InterPro IPR004404:IPR000581; KEGG: fps:FP0449 dihydroxy-acid dehydratase; PFAM: Dihydroxy-acid/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.
  
 0.993
ilvA
Threonine dehydratase; 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.
  
 
 0.946
panB
3-methyl-2-oxobutanoatehydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate; Belongs to the PanB family.
     
 0.907
ADX68205.1
COGs: COG0115 Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase; InterPro IPR001544:IPR005786; KEGG: fba:FIC_01351 branched-chain amino acid aminotransferase; PFAM: Aminotransferase, class IV; PRIAM: Branched-chain-amino-acid transaminase; SPTR: Branched-chain-amino-acid aminotransferase; TIGRFAM: Branched-chain amino acid aminotransferase II; PFAM: Aminotransferase class IV; TIGRFAM: branched-chain amino acid aminotransferase, group II; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
     
 
0.900
ADX68342.1
Aminotransferase class IV; COGs: COG0115 Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase; InterPro IPR001544; KEGG: gfo:GFO_1441 branched-chain-amino-acid aminotransferase; PFAM: Aminotransferase, class IV; SPTR: Branched-chain-amino-acid aminotransferase; PFAM: Aminotransferase class IV.
     
  0.900
ADX66798.1
Acetolactate synthase, large subunit, biosynthetic type; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012846:IPR012001:IPR012000:IPR011766; KEGG: fps:FP0448 acetolactate synthase large subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase; TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N [...]
 
 
 0.892
ADX66799.1
COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR004789:IPR002912:IPR019455; KEGG: fps:FP0447 acetolactate synthase small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT; SPTR: Acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit.
  
 
 0.803
ADX66800.1
COGs: COG0059 Ketol-acid reductoisomerase; InterPro IPR013023:IPR013116:IPR000506; KEGG: fps:FP0446 ketol-acid reductoisomerase; PFAM: Acetohydroxy acid isomeroreductase, catalytic; Acetohydroxy acid isomeroreductase C-terminal; SPTR: Ketol-acid reductoisomerase; TIGRFAM: Acetohydroxy acid isomeroreductase; PFAM: Acetohydroxy acid isomeroreductase, catalytic domain; TIGRFAM: ketol-acid reductoisomerase.
  
  
 0.739
ADX67101.1
Hydroxymethylglutaryl-CoA lyase; COGs: COG0119 Isopropylmalate/homocitrate/citramalate synthase; InterPro IPR000891; KEGG: fjo:Fjoh_2213 pyruvate carboxyltransferase; PFAM: Pyruvate carboxyltransferase; PRIAM: Hydroxymethylglutaryl-CoA lyase; SPTR: Hydroxymethylglutaryl-CoA lyase like protein; PFAM: HMGL-like.
  
 
 0.704
ADX67432.1
Dihydrolipoyllysine-residue acetyltransferase; COGs: COG0508 Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide acyltransferase (E2) protein; InterPro IPR000089:IPR004167:IPR001078; KEGG: fba:FIC_01488 dihydrolipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; PFAM: 2-oxoacid dehydrogenase acyltransferase, catalytic domain; Biotin/lipoyl attachment; E3 binding; PRIAM: Dihydrolipoyllysine-residue acetyltransferase; SPTR: Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalyt [...]
   
 0.553
Your Current Organism:
Weeksella virosa
NCBI taxonomy Id: 865938
Other names: W. virosa DSM 16922, Weeksella virosa ATCC 43766, Weeksella virosa CIP 103040, Weeksella virosa DSM 16922, Weeksella virosa str. DSM 16922, Weeksella virosa strain DSM 16922
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