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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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AEB83009.13-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring); KEGG: pol:Bpro_0273 branched-chain alpha-keto acid dehydrogenase E1 component; PFAM: Dehydrogenase, E1 component; 2-oxoisovalerate dehydrogenase, E1 alpha subunit, N-terminal. (411 aa)    
Predicted Functional Partners:
AEB83010.1
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring); PFAM: Transketolase-like, pyrimidine-binding domain; Transketolase, C-terminal; KEGG: pol:Bpro_0274 branched-chain alpha-keto acid dehydrogenase E1 component; SMART: Transketolase-like, pyrimidine-binding domain.
 0.999
AEB83011.1
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; KEGG: axy:AXYL_02631 lipoamide acyltransferase component of branched-chain alpha-keto aciddehydrogenase complex; PFAM: 2-oxoacid dehydrogenase acyltransferase, catalytic domain; Biotin/lipoyl attachment; E3 binding.
 
 0.998
AEB84781.1
KEGG: dia:Dtpsy_1659 dihydrolipoamide dehydrogenase; TIGRFAM: Dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Biotin/lipoyl attachment; Pyridine nucleotide-disulphide oxidoreductase, dimerisation.
 
 0.998
AEB84892.1
Pyruvate dehydrogenase (acetyl-transferring); PFAM: Transketolase-like, pyrimidine-binding domain; Transketolase, C-terminal; KEGG: rfr:Rfer_3966 transketolase; SMART: Transketolase-like, pyrimidine-binding domain.
 0.998
AEB83012.1
TIGRFAM: Dihydrolipoamide dehydrogenase; KEGG: axy:AXYL_02632 dihydrolipoyl dehydrogenase 2; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation; Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region.
 
 
 0.995
AEB85371.1
TIGRFAM: Dihydrolipoamide dehydrogenase; KEGG: ajs:Ajs_1824 dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region; Pyridine nucleotide-disulphide oxidoreductase, dimerisation.
 
 
 0.974
AEB84890.1
Dihydrolipoyllysine-residue acetyltransferase; KEGG: azo:azo3870 hypothetical protein; PFAM: 2-oxoacid dehydrogenase acyltransferase, catalytic domain.
 
 0.937
ilvE
Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
  
 
 0.917
AEB85372.1
2-oxoglutarate dehydrogenase, E2 subunit, dihydrolipoamide succinyltransferase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).
 
 0.886
AEB84780.1
Pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
 0.878
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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