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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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[Homology]
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Rv0948cProbable mycolyl transferase, pseudogene; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. (105 aa)    
Predicted Functional Partners:
aroG
Phospho-2-dehydro-3-deoxyheptonate aldolase AroG; Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate.
  
 
 0.990
tyrA
Prephenate dehydrogenase TyrA (PDH) (hydroxyphenylpyruvate synthase); Catalyzes the NAD(+)-dependent conversion of prephenate to p- hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E.coli and some other bacteria, that are bifunctional and possess a CM domain.
 
 
 0.970
aroF
Probable chorismate synthase AroF (5-enolpyruvylshikimate-3-phosphate phospholyase); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
  
 
 0.961
Rv1885c
Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.
   
 
 0.952
pheA
Rv3838c, (MTCY01A6.31), len: 321 aa. PheA,prephenate dehydratase (see citation below), equivalent to Q9CDC4|PHEA|ML0078 putative prephenate dehydratase from Mycobacterium leprae (322 aa), FASTA scores: opt: 1690,E(): 1.3e-93, (84.25% identity in 311 aa overlap). Also highly similar to others e.g. P10341|PHEA_CORGL from Corynebacterium glutamicum (Brevibacterium flavum) (315 aa), FASTA scores: opt: 843, E(): 4e-43, (45.8% identity in 308 aa overlap); Q9ZBX0|SCD78.29c from Streptomyces coelicolor (310 aa), FASTA scores: opt: 820, E(): 9.2e-42,(46.45% identity in 312 aa overlap); Q44104|P [...]
  
 
 0.952
trpE
Anthranilate synthase component I TrpE (glutamine amidotransferase); Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly [...]
  
 
 0.948
entC
Probable isochorismate synthase EntC (isochorismate hydroxymutase) (enterochelin biosynthesis); Catalyzes the conversion of chorismate to isochorismate.
  
 
 0.907
trpG
Possible anthranilate synthase component II TrpG (glutamine amidotransferase); Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilat [...]
  
 
 0.892
aroD
3-dehydroquinate dehydratase AroD (AROQ) (3-dehydroquinase) (type II dhqase); Catalyzes a trans-dehydration via an enolate intermediate.
     
 0.832
mbtI
Isochorismate synthase MbtI; Involved in the incorporation of salicylate into the virulence-conferring salicylate-based siderophore mycobactin. Catalyzes the initial conversion of chorismate to yield the intermediate isochorismate (isochorismate synthase activity), and the subsequent elimination of the enolpyruvyl side chain to give salicylate (isochorismate pyruvate-lyase activity). In the absence of magnesium, MbtI displays a chorismate mutase activity and converts chorismate to prephenate.
  
 
 0.823
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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