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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
IQ37_17740Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (707 aa)    
Predicted Functional Partners:
hisI
phosphoribosyl-ATP pyrophosphatase; Catalyzes the formation of 1-(5-phosphoribosyl)-AMP from 1-(5-phosphoribosyl)-ATP and the subsequent formation of 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide from 1-(5-phosphoribosyl)-AMP in histidine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the PRA-CH family.
       0.446
hisF
Imidazole glycerol phosphate synthase; 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.
       0.446
hisA
1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.446
hisH
Imidazole glycerol phosphate synthase; 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.
       0.446
hisB
Imidazoleglycerol-phosphate dehydratase; Catalyzes the formation of 3-(imidazol-4-yl)-2-oxopropyl phosphate from D-ethythro-1-(imidazol-4-yl)glycerol 3-phosphate and histidinol from histidinol phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.
       0.446
hisC
Histidinol phosphate aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
       0.446
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
       0.446
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.
       0.446
IQ37_17640
TetR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.441
IQ37_02605
TonB-dependent receptor; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.419
Your Current Organism:
Chryseobacterium piperi
NCBI taxonomy Id: 558152
Other names: C. piperi, CCUG 57707, Chryseobacterium piperi Strahan et al. 2011 emend. Hahnke et al. 2016, Chryseobacterium sp. CTM, DSM 22249, JCM 15960, KCTC 23267, strain CTM
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