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
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Textmining
[Homology]
Score
ribAGTP cyclohydrolase; Catalyzes the conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate; Belongs to the GTP cyclohydrolase II family. (208 aa)    
Predicted Functional Partners:
OBX07081.1
Riboflavin synthase subunit alpha; Catalyzes the formation of riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.997
ribD
5-amino-6-(5-phosphoribosylamino)uracil reductase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
 0.996
ribB
3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
  
 0.993
ribH
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin; Belongs to the DMRL synthase family.
 
 
 0.992
folE
GTP cyclohydrolase; Involved in the first step of tetrahydrofolate biosynthesis; catalyzes the formation of formate and 2-amino-4-hydroxy-6-(erythro-1,2, 3-trihydroxypropyl)dihydropteridine triphosphate from GTP and water; forms a homopolymer; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 
 0.878
OBX08489.1
Aerobic respiration control protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.811
OBX09474.1
7, 8-dihydro-6-hydroxymethylpterin-pyrophosphokinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.719
ndk
Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family.
  
 0.684
trpF
Indole-3-glycerol phosphate synthase; Monomeric bifunctional protein; functions in tryptophan biosynthesis pathway; phosphoribosylanthranilate is rearranged to carboxyphenylaminodeoxyribulosephosphate which is then closed to form indole-3-glycerol phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TrpC family.
    
 0.651
OBX07515.1
Nucleoside-triphosphate diphosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
     
 0.649
Your Current Organism:
Gallibacterium salpingitidis
NCBI taxonomy Id: 505341
Other names: CCUG 15564, CCUG 36325, G. salpingitidis, Gallibacterium salpingitidis Bisgaard et al. 2009, Gallibacterium sp. 18469/18, Gallibacterium sp. 19987/2, Gallibacterium sp. BK1010/1, Gallibacterium sp. F150, NCTC 11414, strain F150
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