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
OAZ14851.1NAD-glutamate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (1611 aa)    
Predicted Functional Partners:
OAZ14680.1
Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.910
putA
Transcriptional regulator; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.
  
  
 0.904
sucA
SucA; E1 component of the oxoglutarate dehydrogenase complex which catalyzes the formation of succinyl-CoA from 2-oxoglutarate; SucA catalyzes the reaction of 2-oxoglutarate with dihydrolipoamide succinyltransferase-lipoate to form dihydrolipoamide succinyltransferase-succinyldihydrolipoate and carbon dioxide; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.886
OAZ14602.1
Glycine dehydrogenase; Acts in conjunction with GvcH to form H-protein-S-aminomethyldihydrolipoyllysine from glycine; forms a heterodimer with subunit 1 to form the P protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.867
gcvPA
Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
   
 
 0.867
gltA
Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family.
     
 0.867
OAZ14681.1
Dihydropyrimidine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.865
OAZ14256.1
Nitrite reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
    
  0.862
OAZ12515.1
Converts 2-oxoglutarate to glutamate; in Escherichia coli this enzyme plays a role in glutamate synthesis when the cell is under energy restriction; uses NADPH; forms a homohexamer; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.860
OAZ13041.1
5-oxoprolinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.854
Your Current Organism:
Thalassospira profundimaris
NCBI taxonomy Id: 502049
Other names: CGMCC 1.3997, DSM 17430, T. profundimaris, Thalassospira profundimaris Liu et al. 2007, Thalassospira sp. 35, Thalassospira sp. MCCC 1A00350, Thalassospira sp. MCCC 1A00385, Thalassospira sp. MCCC 1A01166, Thalassospira sp. MCCC 1A01318, Thalassospira sp. MCCC 1A02030, Thalassospira sp. PR54-5, Thalassospira sp. R4-5, Thalassospira sp. R8-17, Thalassospira sp. S25-3-2, strain WP0211
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