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
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[Homology]
Score
hisGATP 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. (210 aa)    
Predicted Functional Partners:
hisI
PFAM: Phosphoribosyl-ATP pyrophosphohydrolase; Phosphoribosyl-AMP cyclohydrolase; TIGRFAM: phosphoribosyl-ATP pyrophosphohydrolase; COGs: COG0139 Phosphoribosyl-AMP cyclohydrolase; InterPro IPR002496:IPR021130:IPR008179; KEGG: cyc:PCC7424_2968 bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphatase protein; PFAM: phosphoribosyl-AMP cyclohydrolase; Phosphoribosyl-ATP pyrophosphohydrolase-like; SPTR: Phosphoribosyl-ATP diphosphatase; TIGRFAM: phosphoribosyl-ATP diphosphatase; In the N-terminal section; belongs to the PRA-CH family.
 
 
 0.999
hisZ
histidyl-tRNA synthetase 2; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
 0.999
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.
 
  
 0.983
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
 
  
 0.983
hisB
PFAM: Imidazoleglycerol-phosphate dehydratase; COGs: COG0131 Imidazoleglycerol-phosphate dehydratase; InterPro IPR000807:IPR020565; KEGG: syp:SYNPCC7002_A1985 imidazoleglycerol-phosphate dehydratase; PFAM: imidazoleglycerol-phosphate dehydratase; PRIAM: Imidazoleglycerol-phosphate dehydratase; SPTR: Imidazoleglycerol-phosphate dehydratase.
 
  
 0.982
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.
 
  
 0.980
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 IPR006062:IPR006063; KEGG: cyt:cce_4140 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; PFAM: histidine biosynthesis protein; PRIAM:1-(5-phosphoribosyl)-5-((5-phosphoribosylamin o)methylideneamino)imidazole- [...]
 
  
 0.978
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; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
  
 0.908
hisS
PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase; COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR015807:IPR004516:IPR002314:IPR004154:IPR 006195; KEGG: cyc:PCC7424_5012 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase.
 
 
 0.868
prs
Ribose-phosphate pyrophosphokinase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
  
 
 0.858
Your Current Organism:
Cyanobacterium stanieri
NCBI taxonomy Id: 292563
Other names: C. stanieri PCC 7202, Cyanobacterium stanieri PCC 7202, Synechococcus cedrorum CCAP 14792a (no longer available), Synechococcus cedrorum CCAP 14792b (no longer available), Synechococcus cedrorum M137/1a, Synechococcus cedrorum SAG 88.79, Synechococcus sp. ATCC 29140, Synechococcus sp. PCC 7202
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