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
coaDPantetheine-phosphate adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. (170 aa)    
Predicted Functional Partners:
coaE
dephospho-CoA kinase; Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A; Belongs to the CoaE family.
 
  
 0.974
coaX
Type III pantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
 
  
 0.947
AQS85002.1
Phosphopantothenoylcysteine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.937
gyrA
DNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
 
  
 0.910
guaA
GMP synthetase; Catalyzes the synthesis of GMP from XMP.
 
   
 0.769
AQS83532.1
Riboflavin biosynthesis protein RibF; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ribF family.
 
   
 0.751
AQS84337.1
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.741
ispDF
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D- erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4- diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C- methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
 
   
 0.641
metK
Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
  
   
 0.636
AQS85460.1
Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
       0.623
Your Current Organism:
Acetobacter aceti
NCBI taxonomy Id: 435
Other names: A. aceti, ATCC 15973, Acetimonas aceti, Acetobacter (subgen. Acetobacter) aceti, Acetobacter aceti aceti, Acetobacter aceti orleanensis, Acetobacter aceti subsp. aceti, Acetobacter aceti var. muciparum, Acetobacter ketogenum, Acetobacter lafarianum, Bacillus aceticus, Bacteriopsis aceti, Bacterium aceti, Bacterium acetigenoidum, Bacterium hansenianum, CCUG 18122, CIP 103111, DSM 3508, ICMP 8807, IFO 14818, JCM 7641, Micrococcus aceti, Mycoderma aceti souches non visqueuses (membraneuses), NBRC 14818, NCCB 23001, NCIB 8621, NCIB:8621, NCIMB 8621
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