| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MTH_167 | cbiA | MTH_167 | MTH_1460 | S-adenosyl-L-methionine uroporphyrinogen methyltransferase; Function Code:9.10 - Metabolism of Cofactors and Vitamins, Porphyrin and chlorophyll metabolism; similar to, pir:LN:A42471 AC:A42471, p()=5.9E-84, pid=64%; Belongs to the precorrin methyltransferase family. | Cobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. | 0.858 |
| MTH_167 | hemA | MTH_167 | MTH_1012 | S-adenosyl-L-methionine uroporphyrinogen methyltransferase; Function Code:9.10 - Metabolism of Cofactors and Vitamins, Porphyrin and chlorophyll metabolism; similar to, pir:LN:A42471 AC:A42471, p()=5.9E-84, pid=64%; Belongs to the precorrin methyltransferase family. | glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | 0.762 |
| MTH_167 | hemB | MTH_167 | MTH_744 | S-adenosyl-L-methionine uroporphyrinogen methyltransferase; Function Code:9.10 - Metabolism of Cofactors and Vitamins, Porphyrin and chlorophyll metabolism; similar to, pir:LN:A42471 AC:A42471, p()=5.9E-84, pid=64%; Belongs to the precorrin methyltransferase family. | Porphobilinogen synthase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). | 0.835 |
| MTH_167 | hemC | MTH_167 | MTH_874 | S-adenosyl-L-methionine uroporphyrinogen methyltransferase; Function Code:9.10 - Metabolism of Cofactors and Vitamins, Porphyrin and chlorophyll metabolism; similar to, pir:LN:A42471 AC:A42471, p()=5.9E-84, pid=64%; Belongs to the precorrin methyltransferase family. | Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. | 0.988 |
| MTH_167 | hemD | MTH_167 | MTH_166 | S-adenosyl-L-methionine uroporphyrinogen methyltransferase; Function Code:9.10 - Metabolism of Cofactors and Vitamins, Porphyrin and chlorophyll metabolism; similar to, pir:LN:A42471 AC:A42471, p()=5.9E-84, pid=64%; Belongs to the precorrin methyltransferase family. | Uroporphyrinogen III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. | 0.999 |
| MTH_167 | hemL | MTH_167 | MTH_228 | S-adenosyl-L-methionine uroporphyrinogen methyltransferase; Function Code:9.10 - Metabolism of Cofactors and Vitamins, Porphyrin and chlorophyll metabolism; similar to, pir:LN:A42471 AC:A42471, p()=5.9E-84, pid=64%; Belongs to the precorrin methyltransferase family. | Glutamate-1-semialdehyde aminotransferase; Function Code:9.01 - Metabolism of Cofactors and Vitamins, Thiamine metabolism; similar to, sp:LN:GSA_METJA AC:Q58020, p()=1.9E-135, pid=58%; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily. | 0.683 |
| MTH_743 | hemB | MTH_743 | MTH_744 | Conserved protein; Function Code:14.01 - Unknown, Conserved protein; similar to, sp:LN:Y227_METJA AC:Q57680, p()=1.7E-45, pid=37%. | Porphobilinogen synthase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). | 0.806 |
| MTH_743 | pheS | MTH_743 | MTH_742 | Conserved protein; Function Code:14.01 - Unknown, Conserved protein; similar to, sp:LN:Y227_METJA AC:Q57680, p()=1.7E-45, pid=37%. | phenylalanyl-tRNA synthetase; Function Code:10.07 - Metabolism of Macromolecules, Aminoacyl tRNA synthetases and tRNA modification; similar to, sp:LN:SYF_METJA AC:Q57911, p()=1.9E-93, pid=37%; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily. | 0.871 |
| aroC | fen | MTH_748 | MTH_1633 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | DNA repair protein Rad2; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathwa [...] | 0.438 |
| aroC | hemB | MTH_748 | MTH_744 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Porphobilinogen synthase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). | 0.710 |
| aroC | hemD | MTH_748 | MTH_166 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Uroporphyrinogen III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. | 0.477 |
| aroC | pheS | MTH_748 | MTH_742 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | phenylalanyl-tRNA synthetase; Function Code:10.07 - Metabolism of Macromolecules, Aminoacyl tRNA synthetases and tRNA modification; similar to, sp:LN:SYF_METJA AC:Q57911, p()=1.9E-93, pid=37%; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily. | 0.564 |
| cbiA | MTH_167 | MTH_1460 | MTH_167 | Cobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. | S-adenosyl-L-methionine uroporphyrinogen methyltransferase; Function Code:9.10 - Metabolism of Cofactors and Vitamins, Porphyrin and chlorophyll metabolism; similar to, pir:LN:A42471 AC:A42471, p()=5.9E-84, pid=64%; Belongs to the precorrin methyltransferase family. | 0.858 |
| cbiA | hemA | MTH_1460 | MTH_1012 | Cobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. | glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | 0.995 |
| cbiA | hemB | MTH_1460 | MTH_744 | Cobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. | Porphobilinogen synthase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). | 0.609 |
| cbiA | hemC | MTH_1460 | MTH_874 | Cobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. | Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. | 0.591 |
| cbiA | hemD | MTH_1460 | MTH_166 | Cobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. | Uroporphyrinogen III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. | 0.623 |
| cbiA | hemL | MTH_1460 | MTH_228 | Cobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. | Glutamate-1-semialdehyde aminotransferase; Function Code:9.01 - Metabolism of Cofactors and Vitamins, Thiamine metabolism; similar to, sp:LN:GSA_METJA AC:Q58020, p()=1.9E-135, pid=58%; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily. | 0.560 |
| fen | aroC | MTH_1633 | MTH_748 | DNA repair protein Rad2; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathwa [...] | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | 0.438 |
| fen | hemB | MTH_1633 | MTH_744 | DNA repair protein Rad2; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathwa [...] | Porphobilinogen synthase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). | 0.565 |