| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PMM1692 | PMM1693 | PMM1692 | PMM1693 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | 0.886 |
| PMM1692 | aspS | PMM1692 | PMM1688 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.638 |
| PMM1692 | folP | PMM1692 | PMM0830 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Putative dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. | 0.516 |
| PMM1692 | pabA | PMM1692 | PMM0184 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Para-aminobenzoate synthase component II; CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN; Citation: Kapland and Nichols (1983) J. Mol. Biol. 168:451-468; Tran et al. (1990) J. Bacteriol. 172:397-410; Alternative locus ID: PMED4_01901. | 0.999 |
| PMM1692 | pyrG | PMM1692 | PMM1689 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Glutamine amidotransferase class-I:CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.759 |
| PMM1692 | queC | PMM1692 | PMM1691 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Hypothetical ATPase; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Belongs to the QueC family. | 0.829 |
| PMM1692 | queE | PMM1692 | PMM1690 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Possible organic radical activating enzyme; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. | 0.829 |
| PMM1693 | PMM1692 | PMM1693 | PMM1692 | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | 0.886 |
| PMM1693 | aspS | PMM1693 | PMM1688 | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.640 |
| PMM1693 | folP | PMM1693 | PMM0830 | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | Putative dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. | 0.654 |
| PMM1693 | hisI | PMM1693 | PMM0578 | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | Phosphoribosyl-AMP cyclohydrolase; Alternative locus ID: PMED4_06271; In the C-terminal section; belongs to the PRA-PH family. | 0.629 |
| PMM1693 | ilvD | PMM1693 | PMM0774 | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | Dihydroxy-acid dehydratase; Alternative locus ID: PMED4_08591; Belongs to the IlvD/Edd family. | 0.697 |
| PMM1693 | leuA | PMM1693 | PMM1066 | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.674 |
| PMM1693 | pabA | PMM1693 | PMM0184 | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | Para-aminobenzoate synthase component II; CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN; Citation: Kapland and Nichols (1983) J. Mol. Biol. 168:451-468; Tran et al. (1990) J. Bacteriol. 172:397-410; Alternative locus ID: PMED4_01901. | 0.593 |
| PMM1693 | pyrG | PMM1693 | PMM1689 | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | Glutamine amidotransferase class-I:CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.763 |
| PMM1693 | queC | PMM1693 | PMM1691 | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | Hypothetical ATPase; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Belongs to the QueC family. | 0.834 |
| PMM1693 | queE | PMM1693 | PMM1690 | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | Possible organic radical activating enzyme; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. | 0.831 |
| aspS | PMM1692 | PMM1688 | PMM1692 | Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | 0.638 |
| aspS | PMM1693 | PMM1688 | PMM1693 | Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Aminotransferases class-IV; Hypothetical aminotransferase; Alternative locus ID: PMED4_19041. | 0.640 |
| aspS | pyrG | PMM1688 | PMM1689 | Aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Glutamine amidotransferase class-I:CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.858 |