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.
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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
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hisFImidazole 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. (257 aa)    
Predicted Functional Partners:
hisI
PFAM: Phosphoribosyl-ATP pyrophosphohydrolase; Phosphoribosyl-AMP cyclohydrolase; TIGRFAM: phosphoribosyl-ATP pyrophosphohydrolase; COGs: COG0139 Phosphoribosyl-AMP cyclohydrolase; InterPro IPR008179:IPR002496:IPR021130; KEGG: cyc:PCC7424_2968 bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphatase protein; PFAM: phosphoribosyl-AMP cyclohydrolase; Phosphoribosyl-ATP pyrophosphohydrolase-like; SPTR: Phosphoribosyl-AMP cyclohydrolase domain protein; TIGRFAM: phosphoribosyl-ATP diphosphatase; In the N-terminal section; belongs to the PRA-CH family.
  
 0.999
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.
 0.999
hisB
PFAM: Imidazoleglycerol-phosphate dehydratase; COGs: COG0131 Imidazoleglycerol-phosphate dehydratase; InterPro IPR000807:IPR020565; KEGG: cyh:Cyan8802_0089 imidazoleglycerol-phosphate dehydratase; PFAM: imidazoleglycerol-phosphate dehydratase; PRIAM: Imidazoleglycerol-phosphate dehydratase; SPTR: Imidazoleglycerol-phosphate dehydratase.
 
 
 0.997
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.993
hisA
1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino) imidazole-4-carboxamide isomerase; PFAM: Histidine biosynthesis protein; TIGRFAM: phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; COGs: COG0106 Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase; InterPro IPR006063:IPR006062; KEGG: cyc:PCC7424_4950 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; PFAM: histidine biosynthesis protein; PRIAM:1-(5-phosphoribosyl)-5-((5-phosphoribosylamin o)methylideneamino)imidaz [...]
 
 
0.992
hisG
ATP phosphoribosyltransferase (homohexameric); 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.
 
  
 0.979
hisC
PFAM: Aminotransferase class I and II; TIGRFAM: histidinol-phosphate aminotransferase; COGs: COG0079 Histidinol-phosphate/aromatic aminotransferase and cobyric acid decarboxylase; InterPro IPR004839:IPR005861; KEGG: syp:SYNPCC7002_A0511 histidinol-phosphate aminotransferase; PFAM: aminotransferase class I and II; SPTR: Histidinol-phosphate aminotransferase; TIGRFAM: histidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
  
 0.934
AFZ45562.1
PFAM: Aminotransferase class I and II; TIGRFAM: L-threonine-O-3-phosphate decarboxylase; histidinol-phosphate aminotransferase; COGs: COG0079 Histidinol-phosphate/aromatic aminotransferase and cobyric acid decarboxylase; InterPro IPR005860:IPR004839:IPR004838; KEGG: cyc:PCC7424_0722 threonine-phosphate decarboxylase; PFAM: aminotransferase class I and II; SPTR: L-threonine-O-3-phosphate decarboxylase; TIGRFAM: L-threonine-O-3-phosphate decarboxylase.
 
  
 0.909
hisZ
histidyl-tRNA synthetase 2; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
  
  
 0.885
purH
PFAM: AICARFT/IMPCHase bienzyme; MGS-like domain; TIGRFAM: phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; COGs: COG0138 AICAR transformylase/IMP cyclohydrolase PurH (only IMP cyclohydrolase domain in Aful); InterPro IPR002695:IPR011607:IPR013982; KEGG: cyt:cce_4354 bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PFAM: AICARFT/IMPCHase bienzyme formylation region; MGS domain protein; PRIAM: Phosphoribosylaminoimidazolecarboxamide formyltransferase; SMART: AICARFT/IMPCHase bienzyme formylation region; SPTR: Bifunct [...]
  
 
 0.864
Your Current Organism:
Halothece sp. PCC7418
NCBI taxonomy Id: 65093
Other names: Aphanothece halophytica 7418, Cyanothece sp. PCC 7418, H. sp. PCC 7418, Halothece sp. PCC 7418, Synechococcus sp. ATCC 29534 (no longer available), Synechococcus sp. PCC 7418
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