node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
LI0679 | LI0876 | LI0679 | LI0876 | Xanthosine triphosphate pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function 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. Belongs to the HAM1 NTPase family. | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.655 |
LI0679 | hemN-2 | LI0679 | LI0817 | Xanthosine triphosphate pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function 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. Belongs to the HAM1 NTPase family. | Coproporphyrinogen III oxidase and related Fe-S oxidoreductases; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.568 |
LI0679 | ribD | LI0679 | LI0157 | Xanthosine triphosphate pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function 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. Belongs to the HAM1 NTPase family. | Pyrimidine reductase, riboflavin biosynthesis; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family. | 0.554 |
LI0679 | rimO | LI0679 | LI0678 | Xanthosine triphosphate pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function 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. Belongs to the HAM1 NTPase family. | 2-methylthioadenine synthetase; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | 0.593 |
LI0679 | rlmN | LI0679 | LI0680 | Xanthosine triphosphate pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function 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. Belongs to the HAM1 NTPase family. | Predicted Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.674 |
LI0844 | rlmN | LI0844 | LI0680 | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Predicted Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.550 |
LI0876 | LI0679 | LI0876 | LI0679 | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Xanthosine triphosphate pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function 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. Belongs to the HAM1 NTPase family. | 0.655 |
LI0876 | metG | LI0876 | LI1183 | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.639 |
LI0876 | miaB | LI0876 | LI0821 | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 2-methylthioadenine synthetase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.600 |
LI0876 | ribD | LI0876 | LI0157 | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Pyrimidine reductase, riboflavin biosynthesis; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family. | 0.721 |
LI0876 | rimO | LI0876 | LI0678 | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 2-methylthioadenine synthetase; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | 0.600 |
LI0876 | rlmN | LI0876 | LI0680 | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Predicted Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.916 |
LI0876 | rsmH | LI0876 | LI1097 | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Predicted S-adenosylmethionine-dependent methyltransferase involved in cell envelope biogenesis; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | 0.501 |
hemN-2 | LI0679 | LI0817 | LI0679 | Coproporphyrinogen III oxidase and related Fe-S oxidoreductases; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Xanthosine triphosphate pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function 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. Belongs to the HAM1 NTPase family. | 0.568 |
hemN-2 | rlmN | LI0817 | LI0680 | Coproporphyrinogen III oxidase and related Fe-S oxidoreductases; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Predicted Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.603 |
metG | LI0876 | LI1183 | LI0876 | Methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.639 |
metG | rlmN | LI1183 | LI0680 | Methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | Predicted Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.524 |
metG | trmD | LI1183 | LI0220 | Methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | tRNA-(guanine-N1)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. | 0.607 |
miaB | LI0876 | LI0821 | LI0876 | 2-methylthioadenine synthetase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.600 |
miaB | rlmN | LI0821 | LI0680 | 2-methylthioadenine synthetase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Predicted Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.547 |