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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
Ping_2596KEGG: pca:Pcar_2588 branched-chain amino acid aminotransferase; TIGRFAM: branched-chain amino acid aminotransferase; PFAM: aminotransferase, class IV. (362 aa)    
Predicted Functional Partners:
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 1 subfamily.
  
 0.982
leuA-2
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.
  
 0.982
ilvD
KEGG: vfi:VF2559 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
  
 0.965
ilvD-2
KEGG: lla:L0077 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
  
 0.965
Ping_1275
Aspartate kinase; KEGG: vfi:VF2118 bifunctional aspartokinase I/homeserine dehydrogenase I; TIGRFAM: aspartate kinase; PFAM: aspartate/glutamate/uridylate kinase; homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; In the C-terminal section; belongs to the homoserine dehydrogenase family.
  
 
 0.944
Ping_2782
Pyruvate dehydrogenase complex, E1 beta subunit; PFAM: dehydrogenase, E1 component; Transketolase, central region; Transketolase domain protein; KEGG: bms:BRA0032 acetoin dehydrogenase, alpha/beta subunit, putative.
  
 0.936
panB
Ketopantoate 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.
    
 0.934
Ping_3725
PFAM: aminotransferase, class I and II; KEGG: ppr:PBPRA0054 putative valine-pyruvate aminotransferase.
     
 0.930
Ping_1475
PFAM: aminotransferase, class I and II; KEGG: vvy:VV1114 putative aspartate aminotransferase.
  
 
 0.926
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.
  
 0.910
Your Current Organism:
Psychromonas ingrahamii
NCBI taxonomy Id: 357804
Other names: P. ingrahamii 37, Psychromonas ingrahamii 37, Psychromonas ingrahamii str. 37, Psychromonas ingrahamii strain 37, gas vacuolate str. 37
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