| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MJ_0140 | cbiA | MJ_0140 | MJ_1421 | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | Cobyrinic acid a,c-diamide synthase (cbiA); 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. | 0.595 |
| MJ_0140 | cbiX | MJ_0140 | MJ_0970 | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | Conserved hypothetical protein; Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. 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 insertion of Ni(2+) into sirohydrochlorin to yield Ni- sirohydrochlorin. | 0.985 |
| MJ_0140 | cobA | MJ_0140 | MJ_0965 | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | uroporphyrin-III C-methyltransferase (cobA); Catalyzes both methylations at C-2 and C-7 of uroporphyrinogen III leading to precorrin-1 and precorrin-2; their oxidative esterification gives respectively factor I octamethyl ester and sirohydrochlorin. | 0.996 |
| MJ_0140 | cobS | MJ_0140 | MJ_1438 | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | Cobalamin (5'-phosphate) synthase (cobS); Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family. | 0.495 |
| MJ_0140 | hemA | MJ_0140 | MJ_0143 | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | glutamyl-tRNA reductase (hemA); Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | 0.972 |
| MJ_0140 | hemB | MJ_0140 | MJ_0643 | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | Porphobilinogen synthase (hemB); 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). | 0.736 |
| MJ_0140 | hemC | MJ_0140 | MJ_0569 | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | Porphobilinogen deaminase (hemC); Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. | 0.821 |
| MJ_0140 | hemD | MJ_0140 | MJ_0994 | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | Uroporphyrinogen III synthase (hemD); Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. | 0.758 |
| MJ_0140 | hemL | MJ_0140 | MJ_0603 | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | Glutamate-1-semialdehyde aminotransferase (hemL); Similar to GB:M57676 SP:P30949 PID:143040 GB:AL009126 percent identity: 51.67; identified by sequence similarity; putative; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily. | 0.740 |
| cbiA | MJ_0140 | MJ_1421 | MJ_0140 | Cobyrinic acid a,c-diamide synthase (cbiA); 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. | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | 0.595 |
| cbiA | cbiX | MJ_1421 | MJ_0970 | Cobyrinic acid a,c-diamide synthase (cbiA); 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. | Conserved hypothetical protein; Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. 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 insertion of Ni(2+) into sirohydrochlorin to yield Ni- sirohydrochlorin. | 0.938 |
| cbiA | cobA | MJ_1421 | MJ_0965 | Cobyrinic acid a,c-diamide synthase (cbiA); 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. | uroporphyrin-III C-methyltransferase (cobA); Catalyzes both methylations at C-2 and C-7 of uroporphyrinogen III leading to precorrin-1 and precorrin-2; their oxidative esterification gives respectively factor I octamethyl ester and sirohydrochlorin. | 0.797 |
| cbiA | cobS | MJ_1421 | MJ_1438 | Cobyrinic acid a,c-diamide synthase (cbiA); 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. | Cobalamin (5'-phosphate) synthase (cobS); Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family. | 0.898 |
| cbiA | hemA | MJ_1421 | MJ_0143 | Cobyrinic acid a,c-diamide synthase (cbiA); 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 (hemA); Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | 0.800 |
| cbiA | hemB | MJ_1421 | MJ_0643 | Cobyrinic acid a,c-diamide synthase (cbiA); 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 (hemB); 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). | 0.460 |
| cbiA | hemC | MJ_1421 | MJ_0569 | Cobyrinic acid a,c-diamide synthase (cbiA); 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 (hemC); Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. | 0.416 |
| cbiA | hemD | MJ_1421 | MJ_0994 | Cobyrinic acid a,c-diamide synthase (cbiA); 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 (hemD); Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. | 0.451 |
| cbiA | hemL | MJ_1421 | MJ_0603 | Cobyrinic acid a,c-diamide synthase (cbiA); 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 (hemL); Similar to GB:M57676 SP:P30949 PID:143040 GB:AL009126 percent identity: 51.67; identified by sequence similarity; putative; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily. | 0.411 |
| cbiX | MJ_0140 | MJ_0970 | MJ_0140 | Conserved hypothetical protein; Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. 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 insertion of Ni(2+) into sirohydrochlorin to yield Ni- sirohydrochlorin. | Conserved hypothetical protein; Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity). Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. | 0.985 |
| cbiX | cbiA | MJ_0970 | MJ_1421 | Conserved hypothetical protein; Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. 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 insertion of Ni(2+) into sirohydrochlorin to yield Ni- sirohydrochlorin. | Cobyrinic acid a,c-diamide synthase (cbiA); 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. | 0.938 |
