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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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leuB3-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. (367 aa)    
Predicted Functional Partners:
leuC
Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 0.999
leuD
Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
 
 
 0.998
AMS41793.1
Pfam:pfam10369 Small subunit of acetolactate synthase.
 
 0.996
AMS41792.1
Acetolactate synthase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain.
 
 0.985
AMS39617.1
Putative 2-ketoarginine decarboxylase AruI; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family.
 
 0.975
AMS41690.1
Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family.
 
 0.965
AMS43637.1
Pyridoxal-5-phosphate-dependent protein subunit beta; Pfam:pfam00291 Pyridoxal-phosphate dependent enzyme.
 
 0.956
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.
 
 0.955
AMS40117.1
Decarboxylase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain.
 
 0.953
AMS41455.1
Serine dehydratase; Pfam:pfam00291 Pyridoxal-phosphate dependent enzyme.
 
 0.948
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
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