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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
bkdA12-Oxoisovalerate dehydrogenase, E1 component; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. This complex contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The E1 component displays a modular architecture. The N-terminal domain is a dehydrogenase and the C-terminal domain belongs to the transketolase family. Both activities [...] (658 aa)    
Predicted Functional Partners:
sucB
Dihydrolipoamide succinyltransferase E2 component; 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).
 0.999
bkdA2
2-Oxoisovalerate dehydrogenase, E1 component; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. This complex contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The E1 component displays a modular architecture. The N-terminal domain is a dehydrogenase and the C-terminal domain belongs to the transketolase family. Both activities [...]
 
0.999
bfmBAB
Dihydrolipoyllysine-residue (2-methylpropanoyl) transferase, E2 component; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). This protein is the E2 component and catalyzes the reaction: 2-methylpropanoyl-CoA + enzyme 6-N-(dihydrolipoyl)lysine = CoA + enzyme 6-N-(S-(2-methylpr [...]
 0.999
pdhC
Dihydrolipoyllysine-residue acetyltransferase, PDH complex E2 component; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 0.999
bfmBC
The Dihydrolipoyl dehydrogenase is the E3 component of the branched-chain alpha-keto dehydrogenase complex. This complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. It contains multiple copies of three enzymatic components: branched- chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The E3 component converts the Protein 6-N-(dihydrolipoyl)lysine to protein 6-N-(lipoyl)lysine. Dihydrolipoyl dehydrogenase is a homodimer, which binds 1 NAD [...]
 0.998
pdhD
Dihydrolipoyl dehydrogenase, E3 component; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, linking glycolysis to the tricarboxylic acid cycle. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). PdhD is the E3 component. It catalyzes the oxidation of dihydrolipoamide to lipoamide. PdhD is a homodimer which binds 1 NADP and 1 FAD per subunit; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family; Localiz [...]
 0.997
gorA
Glutathione reductase maintains high levels of reduced glutathione in the cytosol; Its active site is a redox-active disulfide bond; Glutathione reductase is a homodimer which binds 1 NADP and 1 FAD per subunit; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family; Localized in the cytoplasm; High confidence in function and specificity.
 
 0.972
prsA
Ribose-phosphate pyrophosphokinase converts the D-ribose 5-phosphate to 5-phospho-alpha-D-ribose 1-diphosphate in the Pentose phosphate pathway. Utilized by both the de novo and the salvage pathways by which endogenously formed or exogenously added pyrimidine, purine, or pyridine bases are converted to the corresponding ribonucleoside monophosphates; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.949
ilvE
Branched-chain-amino-acid aminotransferase is involved in leucine, isoleucine and valine biosynthesis from L-glutamic acid; It forms a homohexamer and used one Pyridoxal phosphate as cofactor per subunit; Belongs to the Aminotransferase class IV; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.939
datA
D-Amino-acid transaminase acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate prosthetic group to form pyridoxamine and an alpha-keto acid in the first half-reaction. the second half-reaction transferes the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall [...]
  
 0.939
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.