STRINGSTRING
hisD hisD hisA hisA hisB hisB hisG hisG hisC hisC hisI hisI hisE hisE hisH hisH hisF hisF MMP1083 MMP1083 hisH2 hisH2
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. (424 aa)    
Predicted Functional Partners:
hisA
1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Citation: Pfeiffer M, Bestgen H, Burger A, Klein A. (1998). Arch Microbiol 170:418-26.
  
 0.999
hisB
Imidazoleglycerol-phosphate dehydratase; Citation: Tada S, Volrath S, Guyer D, Scheidegger A, Ryals J, Ohta D, Ward E.(1994).Plant Physiol 105:579-83.
  
 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.
  
 0.999
hisC
Histidinol-phosphate aminotransferase; Citation: Conover RK, Doolittle WF. (1990) J Bacteriol 172:3244-9.
  
 0.999
hisI
Phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
 
  
 0.998
hisE
Phosphoribosyl-ATP pyrophosphatase; Citation: Kwon JH, Chun JY, Lee HS, Cheon CI, Song ES, Min KH, Lee MS.(2000) Can J Microbiol.46:848-55.
 
  
 0.996
hisH
Imidazoleglycerol-phosphate synthase, amidotransferase subunit; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of IGP and AICAR (By similarity).
  
 0.973
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.
  
 0.965
MMP1083
Similar to bacterial imidazoleglycerol-phosphate synthase, cyclase subunit; Belongs to the HisA/HisF family.
  
 0.919
hisH2
Similar to bacterial imidazoleglycerol-phosphate synthase, amidotransferase subunit; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of IGP and AICAR (By similarity).
 
  
 0.907
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.