| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEJ60370.1 | AEJ61101.1 | Spith_0083 | Spith_0826 | Hemagluttinin repeat-containing protein; InterPro IPR008619; KEGG: sta:STHERM_c00960 hypothetical protein; PFAM: Filamentous haemagglutinin, bacterial; SPTR: Hemagluttinin repeat-containing protein. | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | 0.475 |
| AEJ60553.1 | AEJ61101.1 | Spith_0267 | Spith_0826 | PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp domain; TIGRFAM: glutamine synthetase, type I; COGs: COG0174 Glutamine synthetase; InterPro IPR008147:IPR008146:IPR004809; KEGG: sta:STHERM_c02830 glutamine synthetase, type 1; PFAM: Glutamine synthetase, catalytic region; Glutamine synthetase, beta-Grasp; SPTR: Glutamine synthetase; TIGRFAM: Glutamine synthetase type I. | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | 0.861 |
| AEJ60553.1 | AEJ61109.1 | Spith_0267 | Spith_0834 | PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp domain; TIGRFAM: glutamine synthetase, type I; COGs: COG0174 Glutamine synthetase; InterPro IPR008147:IPR008146:IPR004809; KEGG: sta:STHERM_c02830 glutamine synthetase, type 1; PFAM: Glutamine synthetase, catalytic region; Glutamine synthetase, beta-Grasp; SPTR: Glutamine synthetase; TIGRFAM: Glutamine synthetase type I. | PFAM: Nitrogen regulatory protein P-II; COGs: COG0347 Nitrogen regulatory protein PII; InterPro IPR002187; KEGG: sta:STHERM_c13230 transcriptional regulatory protein; PFAM: Nitrogen regulatory protein PII; SPTR: Nitrogen regulatory protein P-II. | 0.437 |
| AEJ60553.1 | AEJ61321.1 | Spith_0267 | Spith_1049 | PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp domain; TIGRFAM: glutamine synthetase, type I; COGs: COG0174 Glutamine synthetase; InterPro IPR008147:IPR008146:IPR004809; KEGG: sta:STHERM_c02830 glutamine synthetase, type 1; PFAM: Glutamine synthetase, catalytic region; Glutamine synthetase, beta-Grasp; SPTR: Glutamine synthetase; TIGRFAM: Glutamine synthetase type I. | PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II; COGs: COG0069 Glutamate synthase domain 2; InterPro IPR000583:IPR006982:IPR002932:IPR002489; KEGG: sta:STHERM_c10240 glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal; SPTR: Glutamate synthase (NADH) large subunit. | 0.979 |
| AEJ60553.1 | nadE | Spith_0267 | Spith_0021 | PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp domain; TIGRFAM: glutamine synthetase, type I; COGs: COG0174 Glutamine synthetase; InterPro IPR008147:IPR008146:IPR004809; KEGG: sta:STHERM_c02830 glutamine synthetase, type 1; PFAM: Glutamine synthetase, catalytic region; Glutamine synthetase, beta-Grasp; SPTR: Glutamine synthetase; TIGRFAM: Glutamine synthetase type I. | NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.445 |
| AEJ61101.1 | AEJ60370.1 | Spith_0826 | Spith_0083 | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | Hemagluttinin repeat-containing protein; InterPro IPR008619; KEGG: sta:STHERM_c00960 hypothetical protein; PFAM: Filamentous haemagglutinin, bacterial; SPTR: Hemagluttinin repeat-containing protein. | 0.475 |
| AEJ61101.1 | AEJ60553.1 | Spith_0826 | Spith_0267 | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp domain; TIGRFAM: glutamine synthetase, type I; COGs: COG0174 Glutamine synthetase; InterPro IPR008147:IPR008146:IPR004809; KEGG: sta:STHERM_c02830 glutamine synthetase, type 1; PFAM: Glutamine synthetase, catalytic region; Glutamine synthetase, beta-Grasp; SPTR: Glutamine synthetase; TIGRFAM: Glutamine synthetase type I. | 0.861 |
| AEJ61101.1 | AEJ61103.1 | Spith_0826 | Spith_0828 | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | Methyltransferase type 11; PFAM: Methyltransferase domain; TIGRFAM: biotin biosynthesis protein BioC; InterPro IPR013216; KEGG: sta:STHERM_c13280 biotin biosynthesis protein BioC; PFAM: Methyltransferase type 11; SPTR: Methyltransferase type 11. | 0.559 |
| AEJ61101.1 | AEJ61104.1 | Spith_0826 | Spith_0829 | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | PFAM: Protein of unknown function (DUF452); COGs: COG2830 conserved hypothetical protein; InterPro IPR007398; KEGG: sta:STHERM_c13270 hypothetical protein; PFAM: Protein of unknown function DUF452; SPTR: Putative uncharacterized protein. | 0.559 |
| AEJ61101.1 | AEJ61105.1 | Spith_0826 | Spith_0830 | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | PFAM: Aminotransferase class I and II; TIGRFAM: 8-amino-7-oxononanoate synthase; COGs: COG0156 7-keto-8-aminopelargonate synthetase; InterPro IPR004839; KEGG: sta:STHERM_c13260 hypothetical protein; PFAM: Aminotransferase, class I/II; SPTR: 8-amino-7-oxononanoate synthase. | 0.557 |
| AEJ61101.1 | AEJ61106.1 | Spith_0826 | Spith_0831 | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | PFAM: Aminotransferase class-III; TIGRFAM: adenosylmethionine-8-amino-7-oxononanoate transaminase; COGs: COG0161 Adenosylmethionine-8-amino-7-oxononanoate aminotransferase; InterPro IPR005814; KEGG: sta:STHERM_c13250 adenosylmethionine-8-amino-7-oxononanoate aminotransferase; PFAM: Aminotransferase class-III; SPTR: Adenosylmethionine-8-amino-7-oxononanoate aminotransferase; manually curated; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. | 0.591 |
| AEJ61101.1 | AEJ61109.1 | Spith_0826 | Spith_0834 | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | PFAM: Nitrogen regulatory protein P-II; COGs: COG0347 Nitrogen regulatory protein PII; InterPro IPR002187; KEGG: sta:STHERM_c13230 transcriptional regulatory protein; PFAM: Nitrogen regulatory protein PII; SPTR: Nitrogen regulatory protein P-II. | 0.805 |
| AEJ61101.1 | AEJ61321.1 | Spith_0826 | Spith_1049 | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II; COGs: COG0069 Glutamate synthase domain 2; InterPro IPR000583:IPR006982:IPR002932:IPR002489; KEGG: sta:STHERM_c10240 glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal; SPTR: Glutamate synthase (NADH) large subunit. | 0.719 |
| AEJ61101.1 | bioD | Spith_0826 | Spith_0827 | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | Dethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. | 0.617 |
| AEJ61101.1 | nadE | Spith_0826 | Spith_0021 | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.533 |
| AEJ61103.1 | AEJ61101.1 | Spith_0828 | Spith_0826 | Methyltransferase type 11; PFAM: Methyltransferase domain; TIGRFAM: biotin biosynthesis protein BioC; InterPro IPR013216; KEGG: sta:STHERM_c13280 biotin biosynthesis protein BioC; PFAM: Methyltransferase type 11; SPTR: Methyltransferase type 11. | Glutamate-ammonia ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] | 0.559 |
| AEJ61103.1 | AEJ61104.1 | Spith_0828 | Spith_0829 | Methyltransferase type 11; PFAM: Methyltransferase domain; TIGRFAM: biotin biosynthesis protein BioC; InterPro IPR013216; KEGG: sta:STHERM_c13280 biotin biosynthesis protein BioC; PFAM: Methyltransferase type 11; SPTR: Methyltransferase type 11. | PFAM: Protein of unknown function (DUF452); COGs: COG2830 conserved hypothetical protein; InterPro IPR007398; KEGG: sta:STHERM_c13270 hypothetical protein; PFAM: Protein of unknown function DUF452; SPTR: Putative uncharacterized protein. | 0.941 |
| AEJ61103.1 | AEJ61105.1 | Spith_0828 | Spith_0830 | Methyltransferase type 11; PFAM: Methyltransferase domain; TIGRFAM: biotin biosynthesis protein BioC; InterPro IPR013216; KEGG: sta:STHERM_c13280 biotin biosynthesis protein BioC; PFAM: Methyltransferase type 11; SPTR: Methyltransferase type 11. | PFAM: Aminotransferase class I and II; TIGRFAM: 8-amino-7-oxononanoate synthase; COGs: COG0156 7-keto-8-aminopelargonate synthetase; InterPro IPR004839; KEGG: sta:STHERM_c13260 hypothetical protein; PFAM: Aminotransferase, class I/II; SPTR: 8-amino-7-oxononanoate synthase. | 0.865 |
| AEJ61103.1 | AEJ61106.1 | Spith_0828 | Spith_0831 | Methyltransferase type 11; PFAM: Methyltransferase domain; TIGRFAM: biotin biosynthesis protein BioC; InterPro IPR013216; KEGG: sta:STHERM_c13280 biotin biosynthesis protein BioC; PFAM: Methyltransferase type 11; SPTR: Methyltransferase type 11. | PFAM: Aminotransferase class-III; TIGRFAM: adenosylmethionine-8-amino-7-oxononanoate transaminase; COGs: COG0161 Adenosylmethionine-8-amino-7-oxononanoate aminotransferase; InterPro IPR005814; KEGG: sta:STHERM_c13250 adenosylmethionine-8-amino-7-oxononanoate aminotransferase; PFAM: Aminotransferase class-III; SPTR: Adenosylmethionine-8-amino-7-oxononanoate aminotransferase; manually curated; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. | 0.887 |
| AEJ61103.1 | bioD | Spith_0828 | Spith_0827 | Methyltransferase type 11; PFAM: Methyltransferase domain; TIGRFAM: biotin biosynthesis protein BioC; InterPro IPR013216; KEGG: sta:STHERM_c13280 biotin biosynthesis protein BioC; PFAM: Methyltransferase type 11; SPTR: Methyltransferase type 11. | Dethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. | 0.937 |