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
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[Homology]
Score
dlaTDlaT, dihydrolipoamide acyltransferase, E2 component of pyruvate dehydrogenase; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Appears to be essential for Mtb pathogenesis. (553 aa)    
Predicted Functional Partners:
lpdC
Dihydrolipoyl dehydrogenase; Lipoamide dehydrogenase is an essential component of the alpha-ketoacid dehydrogenase complexes, namely the pyruvate dehydrogenase (PDH) complex, the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, and likely also the 2-oxoglutarate dehydrogenase (ODH) complex. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes. Is also able to catalyze the transhydrogenation of NADH and thio-NAD(+) in the absence of D,L- lipoamide, and the NADH-dependent reduction of [...]
 0.999
aceE
Pyruvate dehydrogenase E1 component; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). AceE has reductase activity with pyruvate but does not react with 2- oxoglutarate.
 
 0.997
kgd
Multifunctional alpha-ketoglutarate metabolic enzyme; Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha- ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy- 3-o [...]
 
0.996
bkdB
Probable branched-chain keto acid dehydrogenase E1 component, beta subunit BkdB; Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched- chain alpha-ketoacids to acyl-CoA and CO(2).
 
 0.993
sucC
Probable succinyl-CoA synthetase (beta chain) SucC (SCS-beta); 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.
  
 0.989
Rv0843
Rv0843, (MTV043.36), len: 334 aa. Probable dehydrogenase, similar to various dehydrogenases e.g. Q46142|Q46142 TPP-dependent acetoin dehydrogenase (326 aa),FASTA scores: opt: 500, E(): 2.4e-26, (32.3% identity in 300 aa overlap); P51267|ODPA_PORPU pyruvate dehydrogenase E1 component from Porphyra purpurea (344 aa), FASTA scores: opt: 451, E(): 4.7e-23, (29.6% identity in 311 aa overlap); etc. Also similar to Rv2497c|pdhA pyruvate dehydrogenase E1 component from Mycobacterium tuberculosis (367 aa).
 
 0.981
bkdA
Probable branched-chain keto acid dehydrogenase E1 component, alpha subunit BkdA; Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched- chain alpha-ketoacids to acyl-CoA and CO(2).
 
 0.981
sucD
Probable succinyl-CoA synthetase (alpha chain) SucD (SCS-alpha); 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.
  
 0.980
lpdA
NAD(P)H quinone reductase LpdA; May contribute to virulence by increasing resistance to reactive oxygen intermediates. It can reduce 2,6-dimethyl-1,4- benzoquinone (DMBQ), 5-hydroxy-1,4-naphthaquinone (5-HNQ) and menadione. NADPH is the physiological reductant rather than NADH.
 0.965
lipA
Probable lipoate biosynthesis protein A LipA; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives; Belongs to the radical SAM superfamily. Lipoyl synthase family.
 
  
 0.949
Your Current Organism:
Mycobacterium tuberculosis H37Rv
NCBI taxonomy Id: 83332
Other names: M. tuberculosis H37Rv, Mycobacterium sp. H37Rv, Mycobacterium tuberculosis str. H37Rv, Mycobacterium tuberculosis strain H37Rv
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