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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
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[Homology]
Score
kgdAlpha-ketoglutarate decarboxylase; Kgd; produces succinic semialdehyde; part of alternative pathway from alpha-ketoglutarate to succinate; essential for normal growth; Derived by automated computational analysis using gene prediction method: Protein Homology. (1148 aa)    
Predicted Functional Partners:
sucC
succinyl-CoA synthetase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
 
 0.999
sucD
succinyl-CoA synthetase subunit alpha; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
 0.999
BF93_06500
Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.997
BF93_01260
Part of four member fumarate reductase enzyme complex FrdABCD which catalyzes the reduction of fumarate to succinate during anaerobic respiration; FrdAB are the catalytic subcomplex consisting of a flavoprotein subunit and an iron-sulfur subunit, respectively; FrdCD are the membrane components which interact with quinone and are involved in electron transfer; the catalytic subunits are similar to succinate dehydrogenase SdhAB; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.995
BF93_02335
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family.
 
 0.995
BF93_01340
Flavoprotein disulfide reductase; Catalyzes the reduction of nonspecific electron acceptors such as 2,6-dimethyl-1,4-benzoquinone and 5-hydroxy-1,4-naphthaquinone; does not have lipoamide dehydrogenase activity; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.991
gcvP
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; Belongs to the GcvP family.
  
 
 0.991
BF93_10490
Pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.991
BF93_18140
Catalyzes the reduction of mycothione or glutathione to mycothione or glutathione disulfide; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.991
BF93_01255
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
  
 0.990
Your Current Organism:
Brachybacterium phenoliresistens
NCBI taxonomy Id: 396014
Other names: B. phenoliresistens, BCRC 17589, Brachybacterium phenoliresistens Chou et al. 2007, Brachybacterium sp. phenol-A, JCM 15157, LMG 23707, LMG:23707, strain phenol-A
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