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
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Gene Fusion
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[Homology]
Score
metHMethionine 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. (912 aa)    
Predicted Functional Partners:
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 [...]
 
 0.999
metF
The 5,10-methylenetetrahydrofolate reductase is involved in the Methionine biosynthesis reducing the 5,10-Methylenetetrahydrofolate to 5-methyltetrahydrofolate. The 5-methyltetrahydrofolate is utilized by methionine synthase to convert homocysteine to methionine; The enzyme is a FAD-containing flavoprotein homotetramer; Belongs to the methylenetetrahydrofolate reductase family; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.992
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 [...]
  
 
 0.957
ahcY
Adenosylhomocysteinase; May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
    
 0.930
metK
S-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.
    
 0.930
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.
  
 
 0.929
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
     
 0.925
metB
The Cystathionine gamma-synthase is found in the Selenoamino acid metabolism pathway and involved in the second step of the methionine biosynthesis; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.924
metC
Cystathionine beta-lyase (CBL) is found in the Selenoamino acids metabolism pathway and in methionine and cysteine biosynthesis pathways. It converts (seleno)cystathionine to (seleno)homocysteine but is also able to catalyze an alpha, gamma elimination; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.924
metZ
O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
  
 
 0.924
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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