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
hisIProbable phosphoribosyl-AMP 1,6 cyclohydrolase HisI; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. (115 aa)    
Predicted Functional Partners:
hisD
Probable histidinol dehydrogenase HisD (HDH); Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
 
  
 0.999
hisB
Rv1601, (MTCY336.03c), len: 210 aa. Probable hisB,imidazole glycerol-phosphate dehydratase. Similar to many e.g. HIS7_STRCO|P16247 from Streptomyces coelicolor (197 aa),FASTA results: opt: 763, E(): 0, (57.4% identity in 202 aa overlap). Belongs to the imidazoleglycerol-phosphate dehydratase family.
 
  
 0.999
hisA
Probable phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase HisA; Involved in both the histidine and tryptophan biosynthetic pathways; Belongs to the HisA/HisF family.
 
 0.999
hisF
Probable cyclase HisF; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity).
 
  
 0.999
hisH
Probable amidotransferase HisH; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF (By similarity).
 
  
 0.998
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.
 
  
 0.996
hisE
Phosphoribosyl-AMP pyrophosphatase HisE; Rv2122c, (MTCY261.18), len: 93 aa. HisE (alternate gene name: irg1), phosphoribosyl-AMP cyclohydrolase (see citation below), similar to many. Note that previously misnamed hisI.
 
 
 0.992
hisG
ATP phosphoribosyltransferase HisG; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).
 
  
 0.983
impA
Probable inositol-monophosphatase ImpA (imp); Catalyzes the dephosphorylation of inositol 1-phosphate (I-1- P) to yield free myo-inositol, a key metabolite in mycobacteria.
  
  
 0.978
gatA
Probable glutamyl-tRNA(GLN) amidotransferase (subunit A) GatA (Glu-ADT subunit A); Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln) (By similarity).
  
  
 0.874
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
Server load: low (30%) [HD]