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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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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
hisBHAMAP: Imidazoleglycerol-phosphate dehydratase; KEGG: mgm:Mmc1_2938 imidazoleglycerol-phosphate dehydratase; PFAM: Imidazoleglycerol-phosphate dehydratase. (194 aa)    
Predicted Functional Partners:
hisC
PFAM: Aminotransferase, class I/II; TIGRFAM: Histidinol-phosphate aminotransferase; HAMAP: Histidinol-phosphate aminotransferase; KEGG: dal:Dalk_0935 histidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
 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.
 
 
 0.998
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.
 
 
 0.998
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.997
hisI
Phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
 
  
 0.985
hisA
1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino) imidazole-4-carboxamide isomerase; PFAM: Histidine biosynthesis; TIGRFAM: Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; HAMAP: 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; KEGG: clj:CLJU_c11710 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4- carboxamide isomerase.
 
  
 0.983
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.
 
  
 0.963
AEH23252.1
TIGRFAM: Histidinol-phosphate phosphatase; HAD-superfamily hydrolase, subfamily IIIA; KEGG: dpr:Despr_1621 histidinol-phosphate phosphatase family protein; PFAM: Haloacid dehalogenase-like hydrolase.
 
 
  
 0.914
AEH23336.1
KEGG: hth:HTH_0871 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal.
  
  
 0.594
argC
N-acetyl-gamma-glutamyl-phosphate reductase; Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.
     
 0.584
Your Current Organism:
Thermodesulfobacterium geofontis
NCBI taxonomy Id: 795359
Other names: T. geofontis OPF15, Thermodesulfobacterium geofontis OPF15, Thermodesulfobacterium sp. OPF15
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