node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Acsm3 | MCBB_0936 | MCBB_0192 | MCBB_0936 | Acyl-coenzyme A synthetase ACSM3, mitochondrial; Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy-and 2,3-or 3,4-unsaturated acids (in vitro). + an acyl-CoA. Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q3UNX5-1; Name=2; IsoId=Q3UNX5-2; Sequence=VSP_028397; Note=No experimental confirmation available; Detected in kidney proximal tubules and in liver. Detected at low [...] | 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 [...] | 0.966 |
Acsm3 | korB | MCBB_0192 | MCBB_0235 | Acyl-coenzyme A synthetase ACSM3, mitochondrial; Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy-and 2,3-or 3,4-unsaturated acids (in vitro). + an acyl-CoA. Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q3UNX5-1; Name=2; IsoId=Q3UNX5-2; Sequence=VSP_028397; Note=No experimental confirmation available; Detected in kidney proximal tubules and in liver. Detected at low [...] | 2-oxoglutarate synthase subunit KorB; sp|O27113|KORB_METTH;evalue=8e-118; PctID=68.88; score=423. | 0.919 |
Acsm3 | porA | MCBB_0192 | MCBB_1789 | Acyl-coenzyme A synthetase ACSM3, mitochondrial; Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy-and 2,3-or 3,4-unsaturated acids (in vitro). + an acyl-CoA. Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q3UNX5-1; Name=2; IsoId=Q3UNX5-2; Sequence=VSP_028397; Note=No experimental confirmation available; Detected in kidney proximal tubules and in liver. Detected at low [...] | Pyruvate synthase subunit PorA; sp|P56810|PORA_METTH;evalue=2e-147; PctID=66.49; score=522. | 0.925 |
Acsm3 | porB | MCBB_0192 | MCBB_1790 | Acyl-coenzyme A synthetase ACSM3, mitochondrial; Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy-and 2,3-or 3,4-unsaturated acids (in vitro). + an acyl-CoA. Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q3UNX5-1; Name=2; IsoId=Q3UNX5-2; Sequence=VSP_028397; Note=No experimental confirmation available; Detected in kidney proximal tubules and in liver. Detected at low [...] | Pyruvate synthase subunit PorB; sp|O27771|PORB_METTH;evalue=2e-143; PctID=83.33; score=508. | 0.925 |
Acsm3 | porC | MCBB_0192 | MCBB_1787 | Acyl-coenzyme A synthetase ACSM3, mitochondrial; Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy-and 2,3-or 3,4-unsaturated acids (in vitro). + an acyl-CoA. Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q3UNX5-1; Name=2; IsoId=Q3UNX5-2; Sequence=VSP_028397; Note=No experimental confirmation available; Detected in kidney proximal tubules and in liver. Detected at low [...] | Pyruvate synthase subunit PorC; sp|O27772|PORC_METTH;evalue=3e-065; PctID=69.49; score=247. | 0.920 |
Acsm3 | porD | MCBB_0192 | MCBB_1788 | Acyl-coenzyme A synthetase ACSM3, mitochondrial; Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy-and 2,3-or 3,4-unsaturated acids (in vitro). + an acyl-CoA. Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q3UNX5-1; Name=2; IsoId=Q3UNX5-2; Sequence=VSP_028397; Note=No experimental confirmation available; Detected in kidney proximal tubules and in liver. Detected at low [...] | Pyruvate synthase subunit PorD; sp|P80903|PORD_METTM;evalue=4e-038; PctID=82.50; score=156. | 0.920 |
MCBB_0936 | Acsm3 | MCBB_0936 | MCBB_0192 | 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 [...] | Acyl-coenzyme A synthetase ACSM3, mitochondrial; Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy-and 2,3-or 3,4-unsaturated acids (in vitro). + an acyl-CoA. Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q3UNX5-1; Name=2; IsoId=Q3UNX5-2; Sequence=VSP_028397; Note=No experimental confirmation available; Detected in kidney proximal tubules and in liver. Detected at low [...] | 0.966 |
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 | porB | MCBB_0936 | MCBB_1790 | 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 PorB; sp|O27771|PORB_METTH;evalue=2e-143; PctID=83.33; score=508. | 0.924 |
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_1791 | MCBB_1792 | MCBB_1791 | MCBB_1792 | Putative ferredoxin MJ0265; sp|Q57713|FER9_METJA;evalue=2e-028; PctID=41.18; score=125. | Putative protein MJ0264; sp|Q57712|Y264_METJA;evalue=2e-026; PctID=48.18; score=117. | 0.998 |
MCBB_1791 | porA | MCBB_1791 | MCBB_1789 | Putative ferredoxin MJ0265; sp|Q57713|FER9_METJA;evalue=2e-028; PctID=41.18; score=125. | Pyruvate synthase subunit PorA; sp|P56810|PORA_METTH;evalue=2e-147; PctID=66.49; score=522. | 0.994 |
MCBB_1791 | porB | MCBB_1791 | MCBB_1790 | Putative ferredoxin MJ0265; sp|Q57713|FER9_METJA;evalue=2e-028; PctID=41.18; score=125. | Pyruvate synthase subunit PorB; sp|O27771|PORB_METTH;evalue=2e-143; PctID=83.33; score=508. | 0.998 |
MCBB_1791 | porC | MCBB_1791 | MCBB_1787 | Putative ferredoxin MJ0265; sp|Q57713|FER9_METJA;evalue=2e-028; PctID=41.18; score=125. | Pyruvate synthase subunit PorC; sp|O27772|PORC_METTH;evalue=3e-065; PctID=69.49; score=247. | 0.954 |
MCBB_1791 | porD | MCBB_1791 | MCBB_1788 | Putative ferredoxin MJ0265; sp|Q57713|FER9_METJA;evalue=2e-028; PctID=41.18; score=125. | Pyruvate synthase subunit PorD; sp|P80903|PORD_METTM;evalue=4e-038; PctID=82.50; score=156. | 0.976 |
MCBB_1792 | MCBB_1791 | MCBB_1792 | MCBB_1791 | Putative protein MJ0264; sp|Q57712|Y264_METJA;evalue=2e-026; PctID=48.18; score=117. | Putative ferredoxin MJ0265; sp|Q57713|FER9_METJA;evalue=2e-028; PctID=41.18; score=125. | 0.998 |
MCBB_1792 | porA | MCBB_1792 | MCBB_1789 | Putative protein MJ0264; sp|Q57712|Y264_METJA;evalue=2e-026; PctID=48.18; score=117. | Pyruvate synthase subunit PorA; sp|P56810|PORA_METTH;evalue=2e-147; PctID=66.49; score=522. | 0.994 |
MCBB_1792 | porB | MCBB_1792 | MCBB_1790 | Putative protein MJ0264; sp|Q57712|Y264_METJA;evalue=2e-026; PctID=48.18; score=117. | Pyruvate synthase subunit PorB; sp|O27771|PORB_METTH;evalue=2e-143; PctID=83.33; score=508. | 0.997 |