node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MCBB_0233 | korA | MCBB_0233 | MCBB_0234 | Putative ferredoxin MJ0146; sp|Q57610|FER3_METJA;evalue=4e-017; PctID=56.45; score=86.7. | 2-oxoglutarate synthase subunit KorA; sp|O27112|KORA_METTH;evalue=3e-152; PctID=70.81; score=538. | 0.992 |
MCBB_0233 | korB | MCBB_0233 | MCBB_0235 | Putative ferredoxin MJ0146; sp|Q57610|FER3_METJA;evalue=4e-017; PctID=56.45; score=86.7. | 2-oxoglutarate synthase subunit KorB; sp|O27113|KORB_METTH;evalue=8e-118; PctID=68.88; score=423. | 0.978 |
MCBB_0233 | korC | MCBB_0233 | MCBB_0236 | Putative ferredoxin MJ0146; sp|Q57610|FER3_METJA;evalue=4e-017; PctID=56.45; score=86.7. | 2-oxoglutarate synthase subunit KorC; sp|P80906|KORC_METTM;evalue=2e-071; PctID=71.04; score=268. | 0.987 |
MCBB_0233 | sucC | MCBB_0233 | MCBB_0237 | Putative ferredoxin MJ0146; sp|Q57610|FER3_METJA;evalue=4e-017; PctID=56.45; score=86.7. | Succinyl-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. | 0.967 |
MCBB_0233 | sucD | MCBB_0233 | MCBB_1593 | Putative ferredoxin MJ0146; sp|Q57610|FER3_METJA;evalue=4e-017; PctID=56.45; score=86.7. | Succinyl-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. | 0.930 |
MCBB_0233 | vorB | MCBB_0233 | MCBB_0194 | Putative ferredoxin MJ0146; sp|Q57610|FER3_METJA;evalue=4e-017; PctID=56.45; score=86.7. | Ketoisovalerate oxidoreductase subunit VorB; sp|O26800|VORB_METTH;evalue=1e-155; PctID=76.86; score=549. | 0.554 |
MCBB_0936 | korA | MCBB_0936 | MCBB_0234 | Acetate-CoA ligase [ADP-forming] I; Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. acetyl-CoA. Kinetic parameters: KM=10 uM for acetyl-CoA; KM=7 uM for ADP; KM=110 uM for phosphate; KM=340 uM for acetate; KM=100 uM for phenylacetate; KM=133 uM for ATP; KM=27 uM for CoA; Note=kc [...] | 2-oxoglutarate synthase subunit KorA; sp|O27112|KORA_METTH;evalue=3e-152; PctID=70.81; score=538. | 0.947 |
MCBB_0936 | korB | MCBB_0936 | MCBB_0235 | Acetate-CoA ligase [ADP-forming] I; Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. acetyl-CoA. Kinetic parameters: KM=10 uM for acetyl-CoA; KM=7 uM for ADP; KM=110 uM for phosphate; KM=340 uM for acetate; KM=100 uM for phenylacetate; KM=133 uM for ATP; KM=27 uM for CoA; Note=kc [...] | 2-oxoglutarate synthase subunit KorB; sp|O27113|KORB_METTH;evalue=8e-118; PctID=68.88; score=423. | 0.954 |
MCBB_0936 | porA | MCBB_0936 | MCBB_1789 | Acetate-CoA ligase [ADP-forming] I; Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. acetyl-CoA. Kinetic parameters: KM=10 uM for acetyl-CoA; KM=7 uM for ADP; KM=110 uM for phosphate; KM=340 uM for acetate; KM=100 uM for phenylacetate; KM=133 uM for ATP; KM=27 uM for CoA; Note=kc [...] | Pyruvate synthase subunit PorA; sp|P56810|PORA_METTH;evalue=2e-147; PctID=66.49; score=522. | 0.947 |
MCBB_0936 | porC | MCBB_0936 | MCBB_1787 | Acetate-CoA ligase [ADP-forming] I; Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. acetyl-CoA. Kinetic parameters: KM=10 uM for acetyl-CoA; KM=7 uM for ADP; KM=110 uM for phosphate; KM=340 uM for acetate; KM=100 uM for phenylacetate; KM=133 uM for ATP; KM=27 uM for CoA; Note=kc [...] | Pyruvate synthase subunit PorC; sp|O27772|PORC_METTH;evalue=3e-065; PctID=69.49; score=247. | 0.913 |
MCBB_0936 | porD | MCBB_0936 | MCBB_1788 | Acetate-CoA ligase [ADP-forming] I; Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. acetyl-CoA. Kinetic parameters: KM=10 uM for acetyl-CoA; KM=7 uM for ADP; KM=110 uM for phosphate; KM=340 uM for acetate; KM=100 uM for phenylacetate; KM=133 uM for ATP; KM=27 uM for CoA; Note=kc [...] | Pyruvate synthase subunit PorD; sp|P80903|PORD_METTM;evalue=4e-038; PctID=82.50; score=156. | 0.913 |
MCBB_0936 | sucC | MCBB_0936 | MCBB_0237 | Acetate-CoA ligase [ADP-forming] I; Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. acetyl-CoA. Kinetic parameters: KM=10 uM for acetyl-CoA; KM=7 uM for ADP; KM=110 uM for phosphate; KM=340 uM for acetate; KM=100 uM for phenylacetate; KM=133 uM for ATP; KM=27 uM for CoA; Note=kc [...] | Succinyl-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. | 0.853 |
MCBB_0936 | sucD | MCBB_0936 | MCBB_1593 | Acetate-CoA ligase [ADP-forming] I; Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. acetyl-CoA. Kinetic parameters: KM=10 uM for acetyl-CoA; KM=7 uM for ADP; KM=110 uM for phosphate; KM=340 uM for acetate; KM=100 uM for phenylacetate; KM=133 uM for ATP; KM=27 uM for CoA; Note=kc [...] | Succinyl-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. | 0.859 |
MCBB_0936 | vorB | MCBB_0936 | MCBB_0194 | Acetate-CoA ligase [ADP-forming] I; Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. acetyl-CoA. Kinetic parameters: KM=10 uM for acetyl-CoA; KM=7 uM for ADP; KM=110 uM for phosphate; KM=340 uM for acetate; KM=100 uM for phenylacetate; KM=133 uM for ATP; KM=27 uM for CoA; Note=kc [...] | Ketoisovalerate oxidoreductase subunit VorB; sp|O26800|VORB_METTH;evalue=1e-155; PctID=76.86; score=549. | 0.503 |
korA | MCBB_0233 | MCBB_0234 | MCBB_0233 | 2-oxoglutarate synthase subunit KorA; sp|O27112|KORA_METTH;evalue=3e-152; PctID=70.81; score=538. | Putative ferredoxin MJ0146; sp|Q57610|FER3_METJA;evalue=4e-017; PctID=56.45; score=86.7. | 0.992 |
korA | MCBB_0936 | MCBB_0234 | MCBB_0936 | 2-oxoglutarate synthase subunit KorA; sp|O27112|KORA_METTH;evalue=3e-152; PctID=70.81; score=538. | Acetate-CoA ligase [ADP-forming] I; Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. acetyl-CoA. Kinetic parameters: KM=10 uM for acetyl-CoA; KM=7 uM for ADP; KM=110 uM for phosphate; KM=340 uM for acetate; KM=100 uM for phenylacetate; KM=133 uM for ATP; KM=27 uM for CoA; Note=kc [...] | 0.947 |
korA | korB | MCBB_0234 | MCBB_0235 | 2-oxoglutarate synthase subunit KorA; sp|O27112|KORA_METTH;evalue=3e-152; PctID=70.81; score=538. | 2-oxoglutarate synthase subunit KorB; sp|O27113|KORB_METTH;evalue=8e-118; PctID=68.88; score=423. | 0.999 |
korA | korC | MCBB_0234 | MCBB_0236 | 2-oxoglutarate synthase subunit KorA; sp|O27112|KORA_METTH;evalue=3e-152; PctID=70.81; score=538. | 2-oxoglutarate synthase subunit KorC; sp|P80906|KORC_METTM;evalue=2e-071; PctID=71.04; score=268. | 0.998 |
korA | porA | MCBB_0234 | MCBB_1789 | 2-oxoglutarate synthase subunit KorA; sp|O27112|KORA_METTH;evalue=3e-152; PctID=70.81; score=538. | Pyruvate synthase subunit PorA; sp|P56810|PORA_METTH;evalue=2e-147; PctID=66.49; score=522. | 0.917 |
korA | porC | MCBB_0234 | MCBB_1787 | 2-oxoglutarate synthase subunit KorA; sp|O27112|KORA_METTH;evalue=3e-152; PctID=70.81; score=538. | Pyruvate synthase subunit PorC; sp|O27772|PORC_METTH;evalue=3e-065; PctID=69.49; score=247. | 0.985 |