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
plsYGlycerol-3-phosphate acyltransferase; TIGRFAM: Membrane protein YgiH; HAMAP: Protein of unknown function DUF205; KEGG: enc:ECL_04385 putative glycerol-3-phosphate acyltransferase PlsY; PFAM: Protein of unknown function DUF205; Belongs to the PlsY family. (204 aa)    
Predicted Functional Partners:
gpsA
KEGG: ent:Ent638_0127 NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; HAMAP: Glycerol-3-phosphate dehydrogenase [NAD(P)+]; PFAM: NAD-dependent glycerol-3-phosphate dehydrogenase, C-terminal; NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal; Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
 
 0.982
plsX
Phosphate acyltransferase; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
 
  
 0.964
aas
Bifunctional protein aas; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
 
 
 0.886
plsB
SMART: Phospholipid/glycerol acyltransferase; TIGRFAM: glycerol-3-phosphate O-acyltransferase; KEGG: enc:ECL_00298 glycerol-3-phosphate acyltransferase; HAMAP: Glycerol-3-phosphate acyltransferase; PFAM: Phospholipid/glycerol acyltransferase; Belongs to the GPAT/DAPAT family.
     
 0.831
eno
Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
    
 0.800
ppc_1
Phosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
     
 0.797
plsC
TIGRFAM: 1-acyl-sn-glycerol-3-phosphate acyltransferase; PFAM: Phospholipid/glycerol acyltransferase; KEGG: enc:ECL_04340 1-acyl-sn-glycerol-3-phosphate acyltransferase; SMART: Phospholipid/glycerol acyltransferase; Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
  
 
 0.793
deoC
Deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate; Belongs to the DeoC/FbaB aldolase family. DeoC type 2 subfamily.
    
 0.792
glpA_1
KEGG: enc:ECL_03533 sn-glycerol-3-phosphate dehydrogenase subunit A; TIGRFAM: Anaerobic glycerol-3-phosphate dehydrogenase, A subunit; PFAM: FAD dependent oxidoreductase; BFD-like [2Fe-2S]-binding region.
     
 0.760
glpD
PFAM: FAD dependent oxidoreductase; KEGG: enc:ECL_04789 glycerol-3-phosphate dehydrogenase; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
     
 0.760
Your Current Organism:
Enterobacter asburiae
NCBI taxonomy Id: 640513
Other names: E. asburiae LF7a, Enterobacter asburiae LF7a, Enterobacter asburiae str. LF7a, Enterobacter asburiae strain LF7a
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