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
metKS-adenosylmethionine synthetase; 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. (418 aa)    
Predicted Functional Partners:
metE
5-Methyltetrahydropteroyltriglutamate- homocysteine methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family.
  
 0.978
metH-2
Methionine synthase, homocysteine-binding module; Methionine synthase or 5-methyltetrahydrofolate-homocysteine S-methyltransferase catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate; L-homocysteine is bound via the zinc atom; Uses the cobalamin (vitamin B12) and zinc as cofactors; This sequence corresponds to the homocysteine-binding domain (Hcy-binding domain) only; Belongs to the vitamin-B12 dependent methionine synthase family; Localize [...]
  
 
 0.932
metH
Methionine synthase, cobalamin-binding module; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
    
 0.930
CAZ95747.1
DNA (cytosine-5-)-methyltransferase specifically methylates the C-5 carbon of cytosines in DNA to produce C5-methylcytosine. It uses S-adenosyl-L-methionine as methyl donor. This protein is highly; High confidence in function and specificity.
    
 0.922
CAZ95227.1
Conserved hypothetical protein; Contains a GAF domain; Localized in the cytoplasm.
     
  0.900
CAZ98368.1
GAF domain-containing protein; Unnamed protein product; Conserved protein belonging to the GAF family. GAF domains are present in phytochromes and cGMP-specific phosphodiesterases. Localized in the cytoplasm; Family membership.
     
  0.900
metX
Homoserine O-acetyltransferase / Aspartokinase / Homoserine dehydrogenase; This enzyme is a modular protein with a homoserine O-acetyltransferase module (N-terminal) that catalyses the homoserine acetylation and belongs to the alpha/beta hydrolase fold family, an aspartate kinase module (central) that catalyzes the phosphorylation of aspartate and belongs to the amino acid kinase family and, in C- terminal part, a homoserine dehydrogenase module that catalyzes the NAD-dependent reduction of aspartate beta- semialdehyde into homoserine. This module is composed of a substrate-binding dom [...]
  
  
 0.811
ribH
Riboflavin synthase beta chain; 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.
  
 
 0.803
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
 
  
 0.796
ahcY
Adenosylhomocysteinase; May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
  
 
 0.779
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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