node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SCM57782.1 | alaS-2 | ING2E5A_1506 | ING2E5A_1507 | Putative protein {ECO:0000313|EMBL:CEA16070,1}; tr|A0A098BZF4|A0A098BZF4_9PORP;evalue=7e-112; PctID=47.22; score=410. | Alanine-tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. diphosphate + L-alanyl-tRNA(Ala). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with [...] | 0.668 |
SCM57782.1 | hsd17b12 | ING2E5A_1506 | ING2E5A_1504 | Putative protein {ECO:0000313|EMBL:CEA16070,1}; tr|A0A098BZF4|A0A098BZF4_9PORP;evalue=7e-112; PctID=47.22; score=410. | Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305}; Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long-and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precurso [...] | 0.509 |
SCM57782.1 | mctR-2 | ING2E5A_1506 | ING2E5A_1510 | Putative protein {ECO:0000313|EMBL:CEA16070,1}; tr|A0A098BZF4|A0A098BZF4_9PORP;evalue=7e-112; PctID=47.22; score=410. | Transcriptional regulatory protein MctR {ECO:0000305}; Member of the two-component regulatory system MctS/MctR, which activates mctP expression; sp|Q1M7A0|MCTR_RHIL3;evalue=8e-010; PctID=51.52; score=64.7. | 0.418 |
SCM57782.1 | mtgA | ING2E5A_1506 | ING2E5A_1508 | Putative protein {ECO:0000313|EMBL:CEA16070,1}; tr|A0A098BZF4|A0A098BZF4_9PORP;evalue=7e-112; PctID=47.22; score=410. | Monofunctional biosynthetic peptidoglycan transglycosylase {ECO:0000255|HAMAP-Rule:MF_00766}; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. | 0.645 |
SCM57782.1 | tcdA | ING2E5A_1506 | ING2E5A_1505 | Putative protein {ECO:0000313|EMBL:CEA16070,1}; tr|A0A098BZF4|A0A098BZF4_9PORP;evalue=7e-112; PctID=47.22; score=410. | tRNA threonylcarbamoyladenosine dehydratase; Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine; sp|O32037|TCDA_BACSU;evalue=8e-034; PctID=33.74; score=144. | 0.508 |
SCM57782.1 | ygbA | ING2E5A_1506 | ING2E5A_1509 | Putative protein {ECO:0000313|EMBL:CEA16070,1}; tr|A0A098BZF4|A0A098BZF4_9PORP;evalue=7e-112; PctID=47.22; score=410. | Putative protein YgbA; sp|P25728|YGBA_ECOLI;evalue=6e-013; PctID=41.38; score=72.8. | 0.418 |
alaS-2 | SCM57782.1 | ING2E5A_1507 | ING2E5A_1506 | Alanine-tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. diphosphate + L-alanyl-tRNA(Ala). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with [...] | Putative protein {ECO:0000313|EMBL:CEA16070,1}; tr|A0A098BZF4|A0A098BZF4_9PORP;evalue=7e-112; PctID=47.22; score=410. | 0.668 |
alaS-2 | hsd17b12 | ING2E5A_1507 | ING2E5A_1504 | Alanine-tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. diphosphate + L-alanyl-tRNA(Ala). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with [...] | Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305}; Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long-and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precurso [...] | 0.446 |
alaS-2 | mctR-2 | ING2E5A_1507 | ING2E5A_1510 | Alanine-tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. diphosphate + L-alanyl-tRNA(Ala). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with [...] | Transcriptional regulatory protein MctR {ECO:0000305}; Member of the two-component regulatory system MctS/MctR, which activates mctP expression; sp|Q1M7A0|MCTR_RHIL3;evalue=8e-010; PctID=51.52; score=64.7. | 0.497 |
alaS-2 | mtgA | ING2E5A_1507 | ING2E5A_1508 | Alanine-tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. diphosphate + L-alanyl-tRNA(Ala). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with [...] | Monofunctional biosynthetic peptidoglycan transglycosylase {ECO:0000255|HAMAP-Rule:MF_00766}; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. | 0.758 |
alaS-2 | tcdA | ING2E5A_1507 | ING2E5A_1505 | Alanine-tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. diphosphate + L-alanyl-tRNA(Ala). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with [...] | tRNA threonylcarbamoyladenosine dehydratase; Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine; sp|O32037|TCDA_BACSU;evalue=8e-034; PctID=33.74; score=144. | 0.479 |
alaS-2 | ygbA | ING2E5A_1507 | ING2E5A_1509 | Alanine-tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. diphosphate + L-alanyl-tRNA(Ala). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with [...] | Putative protein YgbA; sp|P25728|YGBA_ECOLI;evalue=6e-013; PctID=41.38; score=72.8. | 0.477 |
hsd17b12 | SCM57782.1 | ING2E5A_1504 | ING2E5A_1506 | Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305}; Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long-and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precurso [...] | Putative protein {ECO:0000313|EMBL:CEA16070,1}; tr|A0A098BZF4|A0A098BZF4_9PORP;evalue=7e-112; PctID=47.22; score=410. | 0.509 |
hsd17b12 | alaS-2 | ING2E5A_1504 | ING2E5A_1507 | Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305}; Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long-and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precurso [...] | Alanine-tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. diphosphate + L-alanyl-tRNA(Ala). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with [...] | 0.446 |
hsd17b12 | mtgA | ING2E5A_1504 | ING2E5A_1508 | Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305}; Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long-and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precurso [...] | Monofunctional biosynthetic peptidoglycan transglycosylase {ECO:0000255|HAMAP-Rule:MF_00766}; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. | 0.433 |
hsd17b12 | tcdA | ING2E5A_1504 | ING2E5A_1505 | Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305}; Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long-and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precurso [...] | tRNA threonylcarbamoyladenosine dehydratase; Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine; sp|O32037|TCDA_BACSU;evalue=8e-034; PctID=33.74; score=144. | 0.780 |
mctR-2 | SCM57782.1 | ING2E5A_1510 | ING2E5A_1506 | Transcriptional regulatory protein MctR {ECO:0000305}; Member of the two-component regulatory system MctS/MctR, which activates mctP expression; sp|Q1M7A0|MCTR_RHIL3;evalue=8e-010; PctID=51.52; score=64.7. | Putative protein {ECO:0000313|EMBL:CEA16070,1}; tr|A0A098BZF4|A0A098BZF4_9PORP;evalue=7e-112; PctID=47.22; score=410. | 0.418 |
mctR-2 | alaS-2 | ING2E5A_1510 | ING2E5A_1507 | Transcriptional regulatory protein MctR {ECO:0000305}; Member of the two-component regulatory system MctS/MctR, which activates mctP expression; sp|Q1M7A0|MCTR_RHIL3;evalue=8e-010; PctID=51.52; score=64.7. | Alanine-tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. diphosphate + L-alanyl-tRNA(Ala). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with [...] | 0.497 |
mctR-2 | mtgA | ING2E5A_1510 | ING2E5A_1508 | Transcriptional regulatory protein MctR {ECO:0000305}; Member of the two-component regulatory system MctS/MctR, which activates mctP expression; sp|Q1M7A0|MCTR_RHIL3;evalue=8e-010; PctID=51.52; score=64.7. | Monofunctional biosynthetic peptidoglycan transglycosylase {ECO:0000255|HAMAP-Rule:MF_00766}; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. | 0.514 |
mctR-2 | ygbA | ING2E5A_1510 | ING2E5A_1509 | Transcriptional regulatory protein MctR {ECO:0000305}; Member of the two-component regulatory system MctS/MctR, which activates mctP expression; sp|Q1M7A0|MCTR_RHIL3;evalue=8e-010; PctID=51.52; score=64.7. | Putative protein YgbA; sp|P25728|YGBA_ECOLI;evalue=6e-013; PctID=41.38; score=72.8. | 0.811 |