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
mmsAMethylmalonate-semialdehyde dehydrogenase [acylating] (MMSDH), oxidoreductase. (499 aa)    
Predicted Functional Partners:
Lstg_1863
acyl-CoA synthetase.
  
 0.906
Hgd
3-hydroxyisobutyrate dehydrogenase; Belongs to the HIBADH-related family.
 
 
 0.893
acsB
acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
  
 0.880
pta
Phosphate acetyl/butaryl transferase.
  
 
 0.828
putA
Bifunctional PutA protein (proline dehydrogenase/ delta-1-pyrroline-5-carboxylate dehydrogenase); Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.
 
0.800
hmp
Oxidoreductase, FAD-binding protein.
   
 
 0.790
coxB
Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
     
 0.783
Lstg_1386
acyl-CoA synthetase.
  
 0.780
fadH
2,4-dienoyl-CoA reductase.
  
 0.770
pksL_1
Polyketide synthase.
  
 0.767
Your Current Organism:
Legionella steigerwaltii
NCBI taxonomy Id: 460
Other names: ATCC 35302, CCUG 29674, CCUG 56441, CIP 103851, DSM 23076, JCM 7558, L. steigerwaltii, NCTC 11991, strain SC-18-C9
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.