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
odhBDihydrolipoamide S-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). (400 aa)    
Predicted Functional Partners:
odhA
Probable 2-oxoglutarate dehydrogenase. Homology to odhA of A. eutrophus of 63% (sprot|ODO1_ALCEU). THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX CATALYZES THE OVERALL CONVERSION OF 2-OXOGLUTARATE TO SUCCINYL-COA & CO(2). IT CONTAINS MULTIPLE COPIES OF 3 ENZYMATIC COMPONENTS: 2-OXOGLUTARATE DEHYDROGENASE (E1) DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE (E2) AND LIPOAMIDE DEHYDROGENASE (E3). InterPro: Dehydrogenase E1 component (IPR001017); Transletolase (IPR005474) Tigrfam: 2oxo_dh_E1: 2-oxoglutarate dehydrogenase, E1 component Pfam: Dehydrogenase E1 component, Transketolas, pyridine binding domain [...]
 0.999
odhL
Probable dihydrolipoamide dehydrogenase. Homology to odhL of A. eutrophus of 68% (sprot|DLDH_ALCEU). THE BRANCHED-CHAIN ALPHA-KETO DEHYDROGENASE COMPLEX CATALYZES THE OVERALL CONVERSION OF ALPHA-KETO ACIDS TO ACYL-COA AND CO(2). IT CONTAINS MULTIPLE COPIES OF 3 ENZYMATIC COMPONENTS: BRANCHED-CHAIN ALPHA-KETO ACID DECARBOXYLASE (E1) LIPOAMIDE ACYLTRANSFERASE (E2) AND LIPOAMIDE DEHYDROGENASE (E3). InterPro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IPR001327); Pyridine nucleotide-disulphide oxidoreductase, classI (IPR001100); Pyridine nucleotide-disulphide oxidoreducta [...]
 0.999
lpdA
Dihydrolipoamide dehydrogenase. Homology to lpdA of N. meningitides of 70% (trembl|Q59099). THE BRANCHED-CHAIN ALPHA-KETO DEHYDROGENASE COMPLEX CATALYZES THE OVERALL CONVERSION OF ALPHA-KETO ACIDS TO ACYL-COA AND CO(2). IT CONTAINS MULTIPLE COPIES OF 3 ENZYMATIC COMPONENTS: BRANCHED-CHAIN ALPHA-KETO ACID DECARBOXYLASE (E1) LIPOAMIDE ACYLTRANSFERASE (E2) AND LIPOAMIDE DEHYDROGENASE (E3) (BY SIMILARITY). InterPro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IPR001327); Pyridine nucleotide-disulphide oxidoreductase, classI (IPR001100); biotin/Lipoyl attachment (IPR000089) [...]
 0.997
acoB1
Probable acetoin dehydrogenase, beta subunit. Homology to acoB of A. eutrophus of 41% (sprot|ACOB_ALCEU) Catalyzes the 2,6-dichlorophenolindophenol-dependent cleavage of acetoin into acetate and acetaldehyde, in vitro. The beta subunit is probably not the catalytic subunit of the enzyme. Pfam: Transketolase, pyridine binding; Transketolase, C-terminal domain no signal peptide no TMHs; High confidence in function and specificity.
 
 0.989
acoB2
Probable acetoin dehydrogenase, beta subunit. Homology to acoB of. A. eutrophus of 48% (sprot|ACOB_ALCEU) Probable TPP-dependent acetoin dehydrogenase, beta subunit. Homology to acoB of A. eutrophus of 41% (sprot|ACOB_ALCEU) Catalyzes the 2,6-dichlorophenolindophenol-dependent cleavage of acetoin into acetate and acetaldehyde, in vitro. The beta subunit is probably not the catalytic subunit of the enzyme. InterPro: Transketolase (IPR005474) Pfam: Transketoase,pyridine binding domain; Transketolase, C-terminal domain no signal peptide no TMHs; High confidence in function and specificity.
 
 0.989
sucC
Probable succinyl-CoA synthetase, beta chain; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
 
 0.985
sucD
Probable succinyl-CoA synthetase, alpha chain; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
 
 0.983
acoA1
Putative acetoin dehydrogenase, alpha subunit. Homology to acoA of C. magnum of 36% (trembl|Q46142) CATALYZES THE 26-DICHLOROPHENOLINDOPHENOL-DEPENDENT CLEAVAGE OF ACETOIN INTO ACETATE AND ACETALDEHYDE IN VITRO. THE ALPHA SUBUNIT IS PROBABLY THE CATALYTIC SUBUNIT OF THE ENZYME. Pfam: Dehydrogenase E1 component no signal peptide no TMHs; Family membership.
 
 0.976
acoA2
Probable acetoin dehydrogenase, alpha subunit. Homology to acoA of C. magnum of 42% (trembl|Q46142) CATALYZES THE 26-DICHLOROPHENOLINDOPHENOL-DEPENDENT CLEAVAGE OF ACETOIN INTO ACETATE AND ACETALDEHYDE IN VITRO. THE ALPHA SUBUNIT IS PROBABLY THE CATALYTIC SUBUNIT OF THE ENZYME. Pfam: Dehydrogenase E1 component no signal peptide no TMHs; Family membership.
 
 0.976
pdhA
Pyruvate dehydrogenase; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
 0.944
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.