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
ribAGTP cyclohydrolase; Catalyzes the conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. (196 aa)    
Predicted Functional Partners:
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.
 0.998
AKL35985.1
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.
 
 0.994
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.
   
 0.985
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.
 
  
 0.972
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.
 
 
 
 0.963
moaA
Molybdenum cofactor biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate.
     
  0.900
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.
  
 0.853
spoT
(p)ppGpp synthetase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
  
 
  0.816
relA
(p)ppGpp synthetase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
  
 
  0.816
mazG
Nucleoside triphosphate hydrolase; Functions in degradation of stringent response intracellular messenger ppGpp; in Escherichia coli this gene is co-transcribed with the toxin/antitoxin genes mazEF; activity of MazG is inhibited by MazEF in vitro; ppGpp inhibits mazEF expression; MazG thus works in limiting the toxic activity of the MazF toxin induced during starvation; MazG also interacts with the GTPase protein Era; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.804
Your Current Organism:
Klebsiella oxytoca
NCBI taxonomy Id: 571
Other names: ATCC 13182, Bacillus oxytocus perniciosus, CCUG 15717, CIP 103434, DSM 5175, IAM 14201, K. oxytoca, Klebsiella sp. CECRI-24/07, Klebsiella sp. MN9SED2, LMG 3055, LMG:3055, NBRC 102593, NBRC 105695, NCTC 13727, strain 479-2
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