close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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. (439 aa)    
Predicted Functional Partners:
hisB
HAMAP: Imidazoleglycerol-phosphate dehydratase; KEGG: imidazoleglycerol-phosphate dehydratase; PFAM: Imidazoleglycerol-phosphate dehydratase.
 
 0.998
hisF
Imidazole glycerol phosphate synthase subunit 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.
  
 0.993
hisC
PFAM: Aminotransferase, class I/II; TIGRFAM: Histidinol-phosphate aminotransferase; HAMAP: Histidinol-phosphate aminotransferase; KEGG: dba:Dbac_0507 histidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
  
 0.993
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.
  
 0.992
hisI
Phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
 
  
 0.981
hisH
Imidazole glycerol phosphate synthase subunit 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.
 
  
 0.981
hisA
PFAM: Histidine biosynthesis; TIGRFAM: Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; HAMAP: 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; KEGG: dsa:Desal_1557 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase.
 
  
 0.981
hisC-2
PFAM: Aminotransferase, class I/II; TIGRFAM: Histidinol-phosphate aminotransferase; HAMAP: Histidinol-phosphate aminotransferase; KEGG: histidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
  
 0.975
purC
PFAM: SAICAR synthetase; TIGRFAM: SAICAR synthetase; HAMAP: Phosphoribosylaminoimidazole-succinocarboxamide synthase; KEGG: dma:DMR_22050 phosphoribosylaminoimidazole-succinocarboxamide synthase.
 
 
 0.903
cobQ
Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.
  
 0.825
Your Current Organism:
Desulfocurvibacter africanus
NCBI taxonomy Id: 690850
Other names: D. africanus subsp. africanus str. Walvis Bay, Desulfocurvibacter africanus str. Walvis Bay, Desulfocurvibacter africanus subsp. africanus str. Walvis Bay, Desulfovibrio africanus ATCC 19997, Desulfovibrio africanus str. Walvis Bay, Desulfovibrio africanus strain Walvis Bay
Server load: low (20%) [HD]