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
ZMO1745TIGRFAM: methionine synthase; KEGG: swi:Swit_2399 methionine synthase (B12-dependent); PFAM: dihydropteroate synthase DHPS; Methionine synthase B12-binding module cap domain protein; Vitamin B12 dependent methionine synthase activation region; cobalamin B12-binding domain protein. (870 aa)    
Predicted Functional Partners:
ZMO1746
PFAM: homocysteine S-methyltransferase; KEGG: swi:Swit_2400 methionine synthase (B12-dependent).
 
 0.999
ZMO1747
TIGRFAM: 5,10-methylenetetrahydrofolate reductase; KEGG: sal:Sala_0035 5,10-methylenetetrahydrofolate reductase; PFAM: methylenetetrahydrofolate reductase; Belongs to the methylenetetrahydrofolate reductase family.
  
 
 0.991
metE
5- methyltetrahydropteroyltriglutamate/homocysteine S-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.
   
 
 0.947
ZMO0327
KEGG: swi:Swit_3776 cystathionine beta-lyase; TIGRFAM: cystathionine beta-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein; Rhodanese domain protein.
  
 
 0.945
ahcY
Adenosylhomocysteinase; May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
    
 0.942
glyA
Glycine 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.
     
 0.940
fhs
KEGG: mmr:Mmar10_1412 formate-tetrahydrofolate ligase; PFAM: formate-tetrahydrofolate ligase FTHFS; Belongs to the formate--tetrahydrofolate ligase family.
    
 0.939
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.
    
 0.937
ZMO0937
Aromatic-amino-acid transaminase; KEGG: swi:Swit_0763 aromatic amino acid aminotransferase; PFAM: aminotransferase class I and II.
     
 0.910
purH
TIGRFAM: phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; KEGG: swi:Swit_0447 bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PFAM: MGS domain protein; AICARFT/IMPCHase bienzyme formylation region.
     
  0.900
Your Current Organism:
Zymomonas mobilis ZM4
NCBI taxonomy Id: 264203
Other names: Z. mobilis subsp. mobilis ZM4 = ATCC 31821, Zymomonas mobilis subsp. mobilis ATCC 31821, Zymomonas mobilis subsp. mobilis ATCC 31821 = ZM4, Zymomonas mobilis subsp. mobilis ZM4, Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.