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AMD16819.1 AMD16819.1 AMD16922.1 AMD16922.1 porA porA AMD18423.1 AMD18423.1 AMD16924.1 AMD16924.1 AMD17147.1 AMD17147.1 AMD17505.1 AMD17505.1 AMD17537.1 AMD17537.1 sucD sucD AMD17743.1 AMD17743.1 AMD17793.1 AMD17793.1 sucC sucC AMD18141.1 AMD18141.1
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:
AMD16819.1Pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (433 aa)
AMD16922.12-ketoisovalerate ferredoxin oxidoreductase; Catalyzes the coenzyme A-dependent oxidation of 3-methyl-2-oxobutanoate coupled to the reduction of ferredoxin producing S-(2-methylpropanoyl)-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. (288 aa)
porAPyruvate ferredoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (381 aa)
AMD18423.1Pyruvate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (80 aa)
AMD16924.1Pyruvate ferredoxin oxidoreductase; Catalyzes the ferredoxin-dependent oxidative decarboxylation of pyruvate to form acetyl-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. (173 aa)
AMD17147.1acetyl-CoA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. (554 aa)
AMD17505.1Isopropanol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (354 aa)
AMD17537.1Isopropanol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (358 aa)
sucDHypothetical protein; 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. (288 aa)
AMD17743.1acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology. (385 aa)
AMD17793.1acyl-CoA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. (698 aa)
sucCsuccinyl-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. (372 aa)
AMD18141.1Isopropanol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (360 aa)
Your Current Organism:
Methanobrevibacter sp. YE315
NCBI taxonomy Id: 1609968
Other names: M. sp. YE315
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