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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
hisIphosphoribosyl-AMP cyclohydrolase domain protein; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. (127 aa)    
Predicted Functional Partners:
hisA
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; Identified by match to protein family HMM PF00977; match to protein family HMM TIGR00007.
 
 0.999
hisF
Imidazoleglycerol phosphate synthase, cyclase subunit; 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.
  
 0.998
hisB
Imidazoleglycerol-phosphate dehydratase; Identified by match to protein family HMM PF00475.
  
 0.997
hisE
phosphoribosyl-ATP pyrophosphohydrolase; Identified by match to protein family HMM PF01503.
 
 
 0.995
hisH
Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; 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.
 
  
 0.989
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
 
  
 0.989
hisG
ATP phosphoribosyltransferase; 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. Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
 
  
 0.987
hisC
Histidinol-phosphate aminotransferase; Identified by match to protein family HMM PF00155; match to protein family HMM TIGR01141; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
  
 0.984
trpE
Anthranilate synthase component I; 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 from chorismate and high concentr [...]
 
    0.742
SRU_0301
Diaminopimelate decarboxylase; Identified by match to protein family HMM PF00278; match to protein family HMM PF00696; match to protein family HMM PF01842; match to protein family HMM PF02784; match to protein family HMM TIGR00657; match to protein family HMM TIGR01048; Belongs to the Orn/Lys/Arg decarboxylase class-II family.
  
  
 0.714
Your Current Organism:
Salinibacter ruber
NCBI taxonomy Id: 309807
Other names: S. ruber DSM 13855, Salinibacter ruber DSM 13855, Salinibacter ruber str. DSM 13855, Salinibacter ruber strain DSM 13855
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