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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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query proteins and first shell of interactors
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second shell of interactors
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a 3D structure is known or predicted
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hisFPutative 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. (252 aa)    
Predicted Functional Partners:
hisB
KEGG: bth:BT0203 1.6e-181 hisB; histidinol-phosphatase / imidazoleglycerol-phosphate dehydratase K01089:K01693; COG: COG0131 Imidazoleglycerol-phosphate dehydratase; Psort location: Cytoplasmic, score: 8.96; In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.
 
 
 0.999
hisI
Bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphatase protein; KEGG: bth:BT1377 1.1e-95 phosphoribosyl-AMP cyclohydrolase / phosphoribosyl-ATP pyrophosphohydrolase K01496:K01523; COG: COG0139 Phosphoribosyl-AMP cyclohydrolase; Psort location: Cytoplasmic, score: 9.97; In the N-terminal section; belongs to the PRA-CH family.
  
 0.999
hisA
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; KEGG: bth:BT1379 9.2e-106 phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase K01814; COG: COG0106 Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase; Psort location: Cytoplasmic, score: 9.97.
 
0.999
hisH
Putative 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
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.997
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.
 
  
 0.982
hisC
Putative histidinol-phosphate transaminase; KEGG: bth:BT0202 9.0e-163 histidinol-phosphate aminotransferase K00817; COG: COG0079 Histidinol-phosphate/aromatic aminotransferase and cobyric acid decarboxylase; Psort location: Cytoplasmic, score: 8.96; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
  
 0.942
EDV03222.1
Putative threonine-phosphate decarboxylase; KEGG: bfs:BF2523 1.5e-135 putative histidinol-phosphate aminotransferase K00817; COG: COG0079 Histidinol-phosphate/aromatic aminotransferase and cobyric acid decarboxylase; Psort location: Cytoplasmic, score: 8.96.
 
  
 0.844
EDV05368.1
AICARFT/IMPCHase bienzyme; KEGG: xtr:448061 1.2e-119 atic; 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase K00602:K01492; COG: COG0138 AICAR transformylase/IMP cyclohydrolase PurH (only IMP cyclohydrolase domain in Aful); Psort location: Cytoplasmic, score: 8.96.
  
 
 0.831
purH
Phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; KEGG: bfr:BF4101 4.9e-249 phosphoribosylaminoimidazole carboxy formyl formyltransferase K00602:K01492; COG: COG0138 AICAR transformylase/IMP cyclohydrolase PurH (only IMP cyclohydrolase domain in Aful).
  
 
 0.831
Your Current Organism:
Bacteroides intestinalis
NCBI taxonomy Id: 471870
Other names: B. intestinalis DSM 17393, Bacteroides intestinalis 341, Bacteroides intestinalis DSM 17393, Bacteroides intestinalis JCM 13265, Bacteroides intestinalis str. DSM 17393, Bacteroides intestinalis strain DSM 17393
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