node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MJ_0107 | MJ_0108 | MJ_0107 | MJ_0108 | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | Pyruvate kinase; Similar to GB:D13095 SP:Q02499 GB:X57859 PID:285623 percent identity: 38.82; identified by sequence similarity; putative. | 0.936 |
MJ_0107 | MJ_0226 | MJ_0107 | MJ_0226 | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP. Probably functions as a house- cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than X [...] | 0.761 |
MJ_0107 | MJ_0301 | MJ_0107 | MJ_0301 | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | Conserved hypothetical protein; Catalyzes the condensation of 6-hydroxymethyl-7,8- dihydropterin pyrophosphate (DHPP) with 4-(beta-D-ribofuranosyl)- aminobenzene-5'-phosphate (beta-RFA-P) to form 7,8-dihydropterin-6- methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate, a precursor in the biosynthesis of 5,6,7,8-tetrahydromethanopterin (H4MPT). To a lesser extent, is able to condense beta-RFA-P with another arylamine, 1-(4-aminophenyl)-1-deoxy-D-ribitol (APDR), to form 7,8-dihydropterin- 6-methyl-1-(4-aminophenyl)-1-deoxy-D-ribitol. Dephosphorylated beta- RFA-P is not a substrate; [...] | 0.853 |
MJ_0107 | MJ_1427 | MJ_0107 | MJ_1427 | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | Hypothetical protein; Catalyzes the condensation of 4-aminobenzoate (pABA) with 5- phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta- ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P). | 0.817 |
MJ_0107 | mfnB | MJ_0107 | MJ_1099 | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | Conserved hypothetical protein; Catalyzes the formation of 4-(hydroxymethyl)-2- furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P). | 0.938 |
MJ_0107 | mfnD | MJ_0107 | MJ_0815 | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | Conserved hypothetical protein; Catalyzes the formation of an amide bond between tyramine and the gamma carboxy group of L-glutamate. The enzyme also accepts phenylethylamine in vitro. | 0.898 |
MJ_0107 | mfnE | MJ_0107 | MJ_0458 | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | Delta 1-pyrroline-5-carboxylate synthetase; Catalyzes the formation of 5-(aminomethyl)-3-furanmethanol diphosphate (F1-PP) from 5-(aminomethyl)-3-furanmethanol phosphate (F1- P) and ATP. In vitro, can also act as an adenylate kinase that catalyzes the transfer of a phosphoryl group from ATP to AMP, generating two molecules of ADP. | 0.942 |
MJ_0107 | mfnF | MJ_0107 | MJ_0840 | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | Conserved hypothetical protein; Catalyzes the condensation between 5-(aminomethyl)-3- furanmethanol diphosphate (F1-PP) and gamma-glutamyltyramine to produce APMF-Glu. | 0.906 |
MJ_0107 | ribH | MJ_0107 | MJ_0303 | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | Riboflavin synthase beta chain (ribH); Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin; Belongs to the DMRL synthase family. | 0.765 |
MJ_0107 | trpE | MJ_0107 | MJ_1075 | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | Anthranilate synthase component I (trpE); Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high c [...] | 0.789 |
MJ_0108 | MJ_0107 | MJ_0108 | MJ_0107 | Pyruvate kinase; Similar to GB:D13095 SP:Q02499 GB:X57859 PID:285623 percent identity: 38.82; identified by sequence similarity; putative. | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | 0.936 |
MJ_0108 | MJ_0226 | MJ_0108 | MJ_0226 | Pyruvate kinase; Similar to GB:D13095 SP:Q02499 GB:X57859 PID:285623 percent identity: 38.82; identified by sequence similarity; putative. | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP. Probably functions as a house- cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than X [...] | 0.458 |
MJ_0226 | MJ_0107 | MJ_0226 | MJ_0107 | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP. Probably functions as a house- cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than X [...] | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | 0.761 |
MJ_0226 | MJ_0108 | MJ_0226 | MJ_0108 | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP. Probably functions as a house- cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than X [...] | Pyruvate kinase; Similar to GB:D13095 SP:Q02499 GB:X57859 PID:285623 percent identity: 38.82; identified by sequence similarity; putative. | 0.458 |
MJ_0301 | MJ_0107 | MJ_0301 | MJ_0107 | Conserved hypothetical protein; Catalyzes the condensation of 6-hydroxymethyl-7,8- dihydropterin pyrophosphate (DHPP) with 4-(beta-D-ribofuranosyl)- aminobenzene-5'-phosphate (beta-RFA-P) to form 7,8-dihydropterin-6- methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate, a precursor in the biosynthesis of 5,6,7,8-tetrahydromethanopterin (H4MPT). To a lesser extent, is able to condense beta-RFA-P with another arylamine, 1-(4-aminophenyl)-1-deoxy-D-ribitol (APDR), to form 7,8-dihydropterin- 6-methyl-1-(4-aminophenyl)-1-deoxy-D-ribitol. Dephosphorylated beta- RFA-P is not a substrate; [...] | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | 0.853 |
MJ_0301 | ribH | MJ_0301 | MJ_0303 | Conserved hypothetical protein; Catalyzes the condensation of 6-hydroxymethyl-7,8- dihydropterin pyrophosphate (DHPP) with 4-(beta-D-ribofuranosyl)- aminobenzene-5'-phosphate (beta-RFA-P) to form 7,8-dihydropterin-6- methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate, a precursor in the biosynthesis of 5,6,7,8-tetrahydromethanopterin (H4MPT). To a lesser extent, is able to condense beta-RFA-P with another arylamine, 1-(4-aminophenyl)-1-deoxy-D-ribitol (APDR), to form 7,8-dihydropterin- 6-methyl-1-(4-aminophenyl)-1-deoxy-D-ribitol. Dephosphorylated beta- RFA-P is not a substrate; [...] | Riboflavin synthase beta chain (ribH); Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin; Belongs to the DMRL synthase family. | 0.434 |
MJ_1427 | MJ_0107 | MJ_1427 | MJ_0107 | Hypothetical protein; Catalyzes the condensation of 4-aminobenzoate (pABA) with 5- phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta- ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P). | Dihydropteroate synthase; Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6- hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- aminobenzoate to form 7,8-dihydropteroate. | 0.817 |
MJ_1427 | mfnB | MJ_1427 | MJ_1099 | Hypothetical protein; Catalyzes the condensation of 4-aminobenzoate (pABA) with 5- phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta- ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P). | Conserved hypothetical protein; Catalyzes the formation of 4-(hydroxymethyl)-2- furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P). | 0.717 |
MJ_1427 | mfnD | MJ_1427 | MJ_0815 | Hypothetical protein; Catalyzes the condensation of 4-aminobenzoate (pABA) with 5- phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta- ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P). | Conserved hypothetical protein; Catalyzes the formation of an amide bond between tyramine and the gamma carboxy group of L-glutamate. The enzyme also accepts phenylethylamine in vitro. | 0.687 |
MJ_1427 | mfnE | MJ_1427 | MJ_0458 | Hypothetical protein; Catalyzes the condensation of 4-aminobenzoate (pABA) with 5- phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta- ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P). | Delta 1-pyrroline-5-carboxylate synthetase; Catalyzes the formation of 5-(aminomethyl)-3-furanmethanol diphosphate (F1-PP) from 5-(aminomethyl)-3-furanmethanol phosphate (F1- P) and ATP. In vitro, can also act as an adenylate kinase that catalyzes the transfer of a phosphoryl group from ATP to AMP, generating two molecules of ADP. | 0.697 |