| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cbiA,cobB | cobB | PMM1072 | PMM1160 | Putative Cobyrinic acid a,c-diamide synthase; BELONGS TO THE SIRTUIN FAMILY; Citation: Tsang and Escalante-Semerena (1996) J. Bacteriol. 178:7016-7019; Alternative locus ID: PMED4_12181. | Cobyric acid synthase CobB; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | 0.987 |
| cbiA,cobB | cobD | PMM1072 | PMM1316 | Putative Cobyrinic acid a,c-diamide synthase; BELONGS TO THE SIRTUIN FAMILY; Citation: Tsang and Escalante-Semerena (1996) J. Bacteriol. 178:7016-7019; Alternative locus ID: PMED4_12181. | Putative cobalamin biosynthetic protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. | 0.932 |
| cbiA,cobB | cobH | PMM1072 | PMM1646 | Putative Cobyrinic acid a,c-diamide synthase; BELONGS TO THE SIRTUIN FAMILY; Citation: Tsang and Escalante-Semerena (1996) J. Bacteriol. 178:7016-7019; Alternative locus ID: PMED4_12181. | Putative Precorrin-8X methylmutase CobH; Citation: Thibaut et al. (1992) J. Bacteriol. 174:1043-1049; Alternative locus ID: PMED4_18561. | 0.996 |
| cbiA,cobB | hisC/cobC | PMM1072 | PMM0198 | Putative Cobyrinic acid a,c-diamide synthase; BELONGS TO THE SIRTUIN FAMILY; Citation: Tsang and Escalante-Semerena (1996) J. Bacteriol. 178:7016-7019; Alternative locus ID: PMED4_12181. | Aminotransferases class-I; Citation: Crouzet et al. (1990) J. Bacteriol. 172:5968-5979; Alternative locus ID: PMED4_02041. | 0.955 |
| cobB | cbiA,cobB | PMM1160 | PMM1072 | Cobyric acid synthase CobB; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | Putative Cobyrinic acid a,c-diamide synthase; BELONGS TO THE SIRTUIN FAMILY; Citation: Tsang and Escalante-Semerena (1996) J. Bacteriol. 178:7016-7019; Alternative locus ID: PMED4_12181. | 0.987 |
| cobB | cobD | PMM1160 | PMM1316 | Cobyric acid synthase CobB; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | Putative cobalamin biosynthetic protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. | 0.985 |
| cobB | cobH | PMM1160 | PMM1646 | Cobyric acid synthase CobB; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | Putative Precorrin-8X methylmutase CobH; Citation: Thibaut et al. (1992) J. Bacteriol. 174:1043-1049; Alternative locus ID: PMED4_18561. | 0.984 |
| cobB | hisC/cobC | PMM1160 | PMM0198 | Cobyric acid synthase CobB; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | Aminotransferases class-I; Citation: Crouzet et al. (1990) J. Bacteriol. 172:5968-5979; Alternative locus ID: PMED4_02041. | 0.963 |
| cobD | cbiA,cobB | PMM1316 | PMM1072 | Putative cobalamin biosynthetic protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. | Putative Cobyrinic acid a,c-diamide synthase; BELONGS TO THE SIRTUIN FAMILY; Citation: Tsang and Escalante-Semerena (1996) J. Bacteriol. 178:7016-7019; Alternative locus ID: PMED4_12181. | 0.932 |
| cobD | cobB | PMM1316 | PMM1160 | Putative cobalamin biosynthetic protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. | Cobyric acid synthase CobB; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | 0.985 |
| cobD | cobH | PMM1316 | PMM1646 | Putative cobalamin biosynthetic protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. | Putative Precorrin-8X methylmutase CobH; Citation: Thibaut et al. (1992) J. Bacteriol. 174:1043-1049; Alternative locus ID: PMED4_18561. | 0.901 |
| cobD | hisC/cobC | PMM1316 | PMM0198 | Putative cobalamin biosynthetic protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. | Aminotransferases class-I; Citation: Crouzet et al. (1990) J. Bacteriol. 172:5968-5979; Alternative locus ID: PMED4_02041. | 0.816 |
| cobH | cbiA,cobB | PMM1646 | PMM1072 | Putative Precorrin-8X methylmutase CobH; Citation: Thibaut et al. (1992) J. Bacteriol. 174:1043-1049; Alternative locus ID: PMED4_18561. | Putative Cobyrinic acid a,c-diamide synthase; BELONGS TO THE SIRTUIN FAMILY; Citation: Tsang and Escalante-Semerena (1996) J. Bacteriol. 178:7016-7019; Alternative locus ID: PMED4_12181. | 0.996 |
| cobH | cobB | PMM1646 | PMM1160 | Putative Precorrin-8X methylmutase CobH; Citation: Thibaut et al. (1992) J. Bacteriol. 174:1043-1049; Alternative locus ID: PMED4_18561. | Cobyric acid synthase CobB; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | 0.984 |
| cobH | cobD | PMM1646 | PMM1316 | Putative Precorrin-8X methylmutase CobH; Citation: Thibaut et al. (1992) J. Bacteriol. 174:1043-1049; Alternative locus ID: PMED4_18561. | Putative cobalamin biosynthetic protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. | 0.901 |
| cobH | hisC/cobC | PMM1646 | PMM0198 | Putative Precorrin-8X methylmutase CobH; Citation: Thibaut et al. (1992) J. Bacteriol. 174:1043-1049; Alternative locus ID: PMED4_18561. | Aminotransferases class-I; Citation: Crouzet et al. (1990) J. Bacteriol. 172:5968-5979; Alternative locus ID: PMED4_02041. | 0.848 |
| hisB | hisC/cobC | PMM0281 | PMM0198 | Imidazoleglycerol-phosphate dehydratase; Alternative locus ID: PMED4_02861. | Aminotransferases class-I; Citation: Crouzet et al. (1990) J. Bacteriol. 172:5968-5979; Alternative locus ID: PMED4_02041. | 0.839 |
| hisB | hisD | PMM0281 | PMM1488 | Imidazoleglycerol-phosphate dehydratase; Alternative locus ID: PMED4_02861. | Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. | 0.997 |
| hisB | hisF | PMM0281 | PMM0430 | Imidazoleglycerol-phosphate dehydratase; Alternative locus ID: PMED4_02861. | Imidazole glycerol phosphate synthase subunit HisF (cyclase); IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | 0.997 |
| hisB | hisH | PMM0281 | PMM1060 | Imidazoleglycerol-phosphate dehydratase; Alternative locus ID: PMED4_02861. | Glutamine amidotransferase class-I; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. | 0.996 |