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
hisFImidazoleglycerol 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. (253 aa)    
Predicted Functional Partners:
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.
 0.999
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.998
hisB
KEGG: cac:CAC0938 1.4e-54 hisB; imidazoleglycerol-phosphate dehydratase K01693; COG: COG0131 Imidazoleglycerol-phosphate dehydratase; Psort location: Cytoplasmic, score: 8.87.
 
 
 0.998
hisA
KEGG: ath:At2g36230 6.9e-69 F2H17.16; N'-5'-phosphoribosyl-formimino-5-aminoimidazole-4- carboxamide ribonucleotide isomerase K01814; COG: KOG3055 Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase; Psort location: Cytoplasmic, score: 8.87; Belongs to the HisA/HisF family.
  
 
 0.988
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. Short subfamily.
 
  
 0.986
hisE
phosphoribosyl-ATP diphosphatase; KEGG: sao:SAOUHSC_03008 3.6e-56 imidazole glycerol phosphate synthase subunit HisF, putative K01663; COG: COG0139 Phosphoribosyl-AMP cyclohydrolase; Psort location: Cytoplasmic, score: 9.98; In the C-terminal section; belongs to the PRA-PH family.
 
  
0.984
hisZ
ATP phosphoribosyltransferase, regulatory subunit; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
 
  
 0.946
hisC
KEGG: lla:L0065 1.2e-89 hisC; histidinol-phosphate aminotransferase K00817; COG: COG0079 Histidinol-phosphate/aromatic aminotransferase and cobyric acid decarboxylase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
  
 0.885
purH
AICARFT/IMPCHase bienzyme; KEGG: sce:YLR028C 1.4e-125 ADE16; AICAR transformylase/IMP cyclohydrolase K00602:K01492; COG: COG0138 AICAR transformylase/IMP cyclohydrolase PurH (only IMP cyclohydrolase domain in Aful); Psort location: Cytoplasmic, score: 8.87.
  
 
 0.861
apt
Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
   
 
 0.826
Your Current Organism:
Clostridium scindens
NCBI taxonomy Id: 411468
Other names: Clostridium scindens ATCC 35704, [. scindens ATCC 35704, [Clostridium] scindens ATCC 35704
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.