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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Score
hisHImidazole 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. (195 aa)    
Predicted Functional Partners:
hisIE
Histidine biosynthesis bifunctional protein HisIE; HisIE is a bifunctional enzyme containing a N-terminal phosphoribosyl-AMP cyclohydrolase (PRA-CH) domain and a C-terminal phosphoribosyl-ATP pyrophosphatase (PRA-PH) domain, catalyzing the third and second steps of the L-histidine biosynthetic pathway, respectively. PRA-CH catalyzes the reaction: 1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide. It requires Zn ions for activity. PRA-PH catalyzes the reaction: 1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)- [...]
  
 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.
 0.999
hisA
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino) methylideneamino] imidazole-4-carboxamide isomerase; HisA catalyzes the fourth step in the L-histidine biosynthetic pathway: 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide = 5-((5-phospho-1-deoxyribulos-1-ylamino)methylideneamino)- 1-(5-phosphoribosyl)imidazole-4-carboxamide. It forms a monomer and adopts a TIM barrel fold. Display distant similarity with HisF. Localized in the cytoplasm; High confidence in function and specificity.
 
 0.999
hisB
Histidine biosynthesis bifunctional protein HisB; HisB is a bifunctional enzyme containing a N-terminal histidinol-phosphatase (HP) domain and a C-terminal imidazoleglycerol-phosphate dehydratase (IGPD) domain, catalyzing the eighth and sixth steps of L-histidine biosynthetic pathway, respectively. HP catalyzes the dephosphorylation of L-histidinol phosphate. HP forms a homodimer in solution. The active site contains two metal binding sites. IGPD catalyzes the reaction: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O. IGPD is a metalloenz [...]
 
 0.999
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
 
  
 0.988
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.
 
  
 0.988
hisC
The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. Localized in the cytoplasm; High confidence in function and specificity.
 
  
 0.977
purH
Bifunctional enzyme that catalyses the last two steps in de novo purine biosynthesis. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) formyltransferase that catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield 5-formylaminoimidazole-4-carboxamide ribonucleotide (FAICAR) and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase, cyclizing FAICAR to IMP; Belongs to the purH family; Localized in the cytoplasm; High confidence in function and specificity.
    
 0.841
purB
Adenylosuccinate lyase catalyzes step 8 in the pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. It cleaves succinylaminoimidazole carboxamide ribotide into aminoimidazole carboxamide ribotide and fumarate, as well as adenylosuccinate into adenylate and fumarate. Localized in the cytoplasm; High confidence in function and specificity.
    
 0.815
hisC2
The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily; Possibly exported in the periplasmic space by a twin-arginine signal peptide (cleavage site between 32 and 33); High confidence in function and specificity.
 
  
 0.814
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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