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
Swoo_4458PFAM: Methionine synthase vitamin-B12 independent; KEGG: cps:CPS_1151 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase. (342 aa)    
Predicted Functional Partners:
Swoo_4088
Methionine synthase; 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.
  
 
 0.981
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.
  
 0.980
Swoo_0624
KEGG: sse:Ssed_4039 methylenetetrahydrofolate reductase (NAD(P)H); TIGRFAM: 5,10-methylenetetrahydrofolate reductase; PFAM: methylenetetrahydrofolate reductase; Belongs to the methylenetetrahydrofolate reductase family.
  
 0.958
Swoo_0622
O-succinylhomoserine (thiol)-lyase; KEGG: sse:Ssed_4041 cystathionine gamma-synthase; TIGRFAM: O-succinylhomoserine (thiol)-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein.
  
 
 0.952
Swoo_2120
TIGRFAM: cystathionine beta-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein; KEGG: sse:Ssed_2496 cystathionine beta-lyase.
  
 
 0.952
Swoo_3095
Methionine gamma-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein; aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: sse:Ssed_1559 methionine gamma-lyase.
  
 
 0.952
Swoo_4459
PFAM: Domain of unknown function DUF1852; KEGG: vpa:VP1992 hypothetical protein.
 
  
 0.945
Swoo_3427
O-acetylhomoserine/O-acetylserine sulfhydrylase; KEGG: sse:Ssed_3283 O-acetylhomoserine aminocarboxypropyltransferase; TIGRFAM: O-acetylhomoserine/O-acetylserine sulfhydrylase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein; aromatic amino acid beta-eliminating lyase/threonine aldolase.
  
 
 0.942
luxS
Quorum-sensing autoinducer 2 (AI-2), LuxS; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family.
    
 0.939
Swoo_0623
KEGG: sse:Ssed_4040 aspartate kinase, homoserine dehydrogenase; TIGRFAM: aspartate kinase; PFAM: aspartate/glutamate/uridylate kinase; homoserine dehydrogenase; homoserine dehydrogenase NAD-binding; In the C-terminal section; belongs to the homoserine dehydrogenase family.
  
 
 0.936
Your Current Organism:
Shewanella woodyi
NCBI taxonomy Id: 392500
Other names: S. woodyi ATCC 51908, Shewanella woodyi ATCC 51908, Shewanella woodyi str. ATCC 51908, Shewanella woodyi strain ATCC 51908
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.