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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; 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. (286 aa)    
Predicted Functional Partners:
hisI
phosphoribosyl-ATP diphosphatase; COGs: COG0139 Phosphoribosyl-AMP cyclohydrolase; InterPro IPR008179:IPR002496:IPR021130; KEGG: sli:Slin_5481 phosphoribosyl-ATP diphosphatase; PFAM: Phosphoribosyl-ATP pyrophosphohydrolase-like; phosphoribosyl-AMP cyclohydrolase; SPTR: Phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphohydrolase; TIGRFAM: phosphoribosyl-ATP diphosphatase; PFAM: Phosphoribosyl-ATP pyrophosphohydrolase; Phosphoribosyl-AMP cyclohydrolase; TIGRFAM: phosphoribosyl-ATP pyrophosphohydrolase; In the N-terminal section; belongs to the PRA-CH family.
 
 
 0.999
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.999
hisB
COGs: COG0131 Imidazoleglycerol-phosphate dehydratase; InterPro IPR020565:IPR005954:IPR006543:IPR000807; KEGG: dfe:Dfer_2927 imidazole glycerol-phosphate dehydratase/histidinol phosphatase; PFAM: imidazoleglycerol-phosphate dehydratase; PRIAM: Histidinol-phosphatase; SPTR: Histidinol-phosphatase; TIGRFAM: histidinol-phosphatase; histidinol-phosphate phosphatase family protein; PFAM: Imidazoleglycerol-phosphate dehydratase; TIGRFAM: histidinol-phosphate phosphatase family domain; histidinol-phosphatase; In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.
 
  
 0.998
hisC
COGs: COG0079 Histidinol-phosphate/aromatic aminotransferase and cobyric acid decarboxylase; InterPro IPR005861:IPR001917:IPR004839; KEGG: dfe:Dfer_1138 histidinol-phosphate aminotransferase; PFAM: aminotransferase class I and II; SPTR: Histidinol-phosphate aminotransferase; TIGRFAM: histidinol-phosphate aminotransferase; PFAM: Aminotransferase class I and II; TIGRFAM: histidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
  
 0.993
hisA
COGs: COG0106 Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase; InterPro IPR006062:IPR006063; KEGG: dfe:Dfer_4238 phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; PFAM: histidine biosynthesis protein; SPTR:1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; TIGRFAM: phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; PFAM: Histidine biosynthesis protein; TIGRFAM: phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase.
 
  
 0.987
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.
 
  
 0.987
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.
 
  
 0.986
hisS
COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195:IPR015807:IPR004516:IPR002314:IPR 004154; KEGG: dfe:Dfer_1143 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; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase.
  
 
 0.903
Lbys_0631
COGs: COG0527 Aspartokinase; InterProIPR018042:IPR019811:IPR011147:IPR001048:IPR 002912:IPR005106:IPR001342:IPR001341; KEGG: sli:Slin_4514 aspartate kinase; PFAM: homoserine dehydrogenase; aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; PRIAM: Aspartate kinase., Homoserine dehydrogenase; SPTR: Aspartate kinase; TIGRFAM: aspartate kinase; PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain; Amino acid kinase family; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase.
 
  
 0.895
Lbys_0088
Ribose-phosphate pyrophosphokinase; COGs: COG0462 Phosphoribosylpyrophosphate synthetase; InterPro IPR000842:IPR005946:IPR000836; KEGG: dfe:Dfer_0421 ribose-phosphate pyrophosphokinase; PFAM: phosphoribosyltransferase; PRIAM: Ribose-phosphate diphosphokinase; SPTR: Ribose-phosphate pyrophosphokinase; TIGRFAM: ribose-phosphate pyrophosphokinase; PFAM: Phosphoribosyl transferase domain; TIGRFAM: ribose-phosphate pyrophosphokinase.
  
 
 0.856
Your Current Organism:
Leadbetterella byssophila
NCBI taxonomy Id: 649349
Other names: L. byssophila DSM 17132, Leadbetterella byssophila 4M15, Leadbetterella byssophila DSM 17132, Leadbetterella byssophila str. DSM 17132, Leadbetterella byssophila strain DSM 17132
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