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HX89_10850 protein (Dermacoccus nishinomiyaensis) - STRING interaction network
"HX89_10850" - Methylmalonyl-CoA mutase in Dermacoccus nishinomiyaensis
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
Score
HX89_10850Methylmalonyl-CoA mutase; Derived by automated computational analysis using gene prediction method- Protein Homology (155 aa)    
Predicted Functional Partners:
HX89_10585
Methylmalonyl-CoA mutase; Derived by automated computational analysis using gene prediction method- Protein Homology (532 aa)
  0.998
HX89_04935
Glyoxalase; Derived by automated computational analysis using gene prediction method- Protein Homology (149 aa)
   
  0.996
HX89_04945
Transporter; Derived by automated computational analysis using gene prediction method- Protein Homology (316 aa)
 
 
  0.985
sucC
Succinate--CoA ligase [ADP-forming] 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 (394 aa)
       
    0.969
sucD
Succinate--CoA ligase [ADP-forming] 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 (299 aa)
       
    0.967
gltA
Citrate synthase; 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 [...] (421 aa)
       
  0.832
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate (327 aa)
       
  0.820
HX89_09995
Pyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second (1126 aa)
         
  0.814
HX89_06035
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; Derived by automated computational analysis using gene prediction method- Protein Homology (616 aa)
       
    0.802
HX89_02120
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; Derived by automated computational analysis using gene prediction method- Protein Homology (488 aa)
       
    0.802
Your Current Organism:
Dermacoccus nishinomiyaensis
NCBI taxonomy Id: 1274
Other names: ATCC 29093, CCM 2140, CCUG 33028, CIP 81.71, D. nishinomiyaensis, DSM 20448, Dermacoccus nishinomiyaensis, Dermacoccus nishinomiyensis, Dermatococcus nishinomiyaensis, Dermatococcus nishinomiyensis, IEGM 393, IFO 15356, JCM 11613, LMG 14222, Micrococcus nishinomiyaensis, Micrococcus nishinomyaensis, NBRC 15356, NCTC 11039
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