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
pheARv3838c, (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 [...] (321 aa)    
Predicted Functional Partners:
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.
 
 0.992
Rv0948c
Probable mycolyl transferase, pseudogene; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.
  
 
 0.940
Rv1885c
Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.
  
 
 0.937
hisC1
Rv1600, (MTCY336.04c), len: 380 aa. Probable hisC1,histidinol-phosphate aminotransferase O06591. Similar to many e.g. HIS8_STRCO|P16246 from Streptomyces coelicolor (369 aa), FASTA results: opt: 1353, E(): 0, (59.0% identity in 356 aa overlap). Some similarity to other Mycobacterium tuberculosis aminotransferases e.g. Rv3772|MTCY13D12.06,FASTA results: E(): 7.4e-25, (33.7% identity in 365 aa overlap). Contains aminotransferases class-II pyridoxal-phosphate attachment site (PS00599). Belongs to class-II of pyridoxal-phosphate-dependent aminotransferases. Note that previously known as hisC.
  
 
 0.916
cobC
Rv2231c, (MTCY427.12c), len: 364 aa. Possible cobC,aminotransferase. Note that initiation codon uncertain. Similar to CobC aminotransferases e.g. sp|P21633|COBC_PSEDE COBC protein (333 aa) opt: 277, E(): 1.7e-11; 28.8% identity in 313 aa overlap and also to e.g. SW:HIS8_ECOLI P06986 histidinol-phosphate aminotransferase (27.0% identity in 289 aa overlap), contains PS00105 aminotransferases class-I pyridoxal-phosphate attachment site. Real Mycobacterium tuberculosis histidinol-phosphate aminotransferase, hisC, is Rv1600 (MTCY336.04c); Belongs to the class-I pyridoxal-phosphate-dependent [...]
  
 
 0.916
hisC2
Putative phenylalanine aminotransferase; May catalyze the transamination reaction in phenylalanine biosynthesis; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
  
 
 0.916
Rv3837c
Rv3837c, (MTCY01A6.32), len: 232 aa. Probable phosphoglycerate mutase, equivalent to Q9CDC3|ML0079 putative phosphoglycerate mutase from Mycobacterium leprae (231 aa), FASTA scores: opt: 1116, E(): 7.3e-66, (71.55% identity in 232 aa overlap). Also similar to others e.g. Q9ZAX0|PGM 2,3-PDG dependent phosphoglycerate mutase from Amycolatopsis methanolica (205 aa), FASTA scores: opt: 474,E(): 6.4e-24, (41.85% identity in 203 aa overlap); Q9F3Q7|SC10F4.03 putative isomerase from Streptomyces coelicolor (224 aa) FASTA scores: opt: 349, E(): 1e-15,(33.2% identity in 223 aa overlap); Q9RDL0| [...]
  
    0.884
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.
 
  
 0.830
katG
Catalase-peroxidase-peroxynitritase T KatG; Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity, oxidizing various electron donors including NADP(H). Protects M.tuberculosis against toxic reactive oxygen species (ROS) including hydrogen peroxide as well as organic peroxides and thus contributes to its survival within host macrophages by countering the phagocyte oxidative burst. Also displays efficient peroxynitritase activity, which may help the bacterium to persist in macrophages. Catalyzes the oxidative activation of the antitubercular pro- drug isoniazid (I [...]
   
 
  0.801
Rv3839
Rv3839, (MTCY01A6.30c), len: 258 aa. Conserved hypothetical protein, similar in part to Q9RD78|SCF43.10cfrom hypothetical 25.8 KDA protein Streptomyces coelicolor (241 aa), FASTA scores: opt: 270,E(): 3.2e-10, (33.45% identity in 272 aa overlap); and O00320|F25451_2 hypothetical protein from Homo sapiens (Human) (339 aa), FASTA scores: opt: 126, E(): 0.77,(28.75% identity in 240 aa overlap).
  
    0.784
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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