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
hisDHistidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. (433 aa)    
Predicted Functional Partners:
hisF
Imidazole glycerol phosphate synthase; 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.
  
 0.999
hisH
Hypothetical protein; 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.
  
 0.999
hisB
Imidazoleglycerol-phosphate dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.999
hisC
Histidinol-phosphate aminotransferase; Catalyzes the formation of L-histidinol phosphate from imidazole-acetol phosphate and glutamate in histidine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
  
 0.999
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.
  
 0.998
hisA
Phosphoribosyl isomerase; Catalyzes the formation of 5-(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino-l- (5-phosphoribosyl)imidazole-4-carboxamide from 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide and the formation of 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate from N-(5-phospho-beta-D-ribosyl)anthranilate; involved in histidine and tryptophan biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.996
hisI
phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
 
  
 0.992
hisE
phosphoribosyl-ATP pyrophosphatase; Catalyzes the formation of 1-(5-phosphoribosyl)-AMPfrom 1-(5-phosphoribolsyl)-ATP in histidine biosynthesis;Derived by automated computational analysis using geneprediction method: Protein Homology.
 
  
 0.981
pat
Aminotransferase; May catalyze the transamination reaction in phenylalanine biosynthesis; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
  
 0.969
cobB
CobB cobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L- glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family.
 
  
 0.766
Your Current Organism:
Aeromicrobium erythreum
NCBI taxonomy Id: 2041
Other names: A. erythreum, ATCC 51598, DSM 8599, JCM 8359, LMG 16472, LMG:16472, NBRC 15406, NRRL B-3381
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