STRINGSTRING
ABK71627.1 ABK71627.1 ilvC ilvC ilvE ilvE leuA leuA ABK73567.1 ABK73567.1 ilvD-2 ilvD-2 panB panB ilvD ilvD ilvN ilvN ilvB ilvB ilvA ilvA
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
ABK71627.1Dihydroxy-acid dehydratase; Identified by match to protein family HMM PF00920; Belongs to the IlvD/Edd family. (564 aa)    
Predicted Functional Partners:
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.
 
 
 0.996
ilvE
Branched-chain amino acid aminotransferase; Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
 
 0.976
leuA
2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
 
 
 0.963
ABK73567.1
Aspartate aminotransferase; Identified by match to protein family HMM PF00155.
  
 
 0.923
ilvD-2
Dihydroxy-acid dehydratase; Identified by match to protein family HMM PF00920; match to protein family HMM TIGR00110; Belongs to the IlvD/Edd family.
  
 
 
0.922
panB
3-methyl-2-oxobutanoate hydroxymethyltransferase; 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.
  
 
 0.919
ilvD
Dihydroxy-acid dehydratase; Identified by match to protein family HMM PF00920; match to protein family HMM TIGR00110; Belongs to the IlvD/Edd family.
  
 
 
0.917
ilvN
Acetolactate synthase, small subunit; Identified by match to protein family HMM PF01842; match to protein family HMM TIGR00119; Belongs to the acetolactate synthase small subunit family.
 
 
 0.917
ilvB
Acetolactate synthase, large subunit, biosynthetic type; Identified by match to protein family HMM PF00205; match to protein family HMM PF02775; match to protein family HMM PF02776; match to protein family HMM TIGR00118.
  
 0.916
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.
 
  
 0.891
Your Current Organism:
Mycolicibacterium smegmatis
NCBI taxonomy Id: 246196
Other names: M. smegmatis MC2 155, Mycobacterium smegmatis MC2 155, Mycolicibacterium smegmatis MC2 155
Server load: low (28%) [HD]