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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
AEB82526.1Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. (207 aa)    
Predicted Functional Partners:
psd
Phosphatidylserine decarboxylase proenzyme; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
 
 
 0.949
AEB84014.1
TIGRFAM: CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; KEGG: dia:Dtpsy_1186 CDP-diacylglycerol/glycerol-3-phosphate 3-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
  
 
 0.925
AEB85470.1
KEGG: xtr:100496448 CDP-diacylglycerol--serine O-phosphatidyltransferase-like; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
  
  
 
0.923
AEB85795.1
PFAM: Phosphatidate cytidylyltransferase; KEGG: dia:Dtpsy_1228 phosphatidate cytidylyltransferase; Belongs to the CDS family.
    
 0.921
AEB82560.1
L-serine dehydratase 1; TIGRFAM: Iron-sulphur-dependent L-serine dehydratase single chain form; KEGG: dia:Dtpsy_0112 L-serine dehydratase 1; PFAM: Serine dehydratase-like, alpha subunit; Serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
 
  
  0.915
AEB86586.1
Phospholipase A(1); Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Belongs to the phospholipase A1 family.
  
  
  0.911
AEB85950.1
TIGRFAM: Phosphoserine phosphatase SerB; HAD-superfamily hydrolase, subfamily IB, PSPase-like; KEGG: dia:Dtpsy_2506 phosphoserine phosphatase SerB; PFAM: Haloacid dehalogenase-like hydrolase.
    
 0.905
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.
    
 0.904
AEB82543.1
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
    
  0.903
ilvA
Threonine dehydratase, biosynthetic; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
    
  0.903
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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