node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SIT70292.1 | SIT70455.1 | SAMN05216526_1280 | SAMN05216526_1317 | Glutamate synthase (NADH) large subunit. | Coproporphyrinogen III oxidase, anaerobic; 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. | 0.573 |
SIT70292.1 | SIT70459.1 | SAMN05216526_1280 | SAMN05216526_1318 | Glutamate synthase (NADH) large subunit. | XTP/dITP diphosphohydrolase; 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. | 0.642 |
SIT70292.1 | SIT70468.1 | SAMN05216526_1280 | SAMN05216526_1320 | Glutamate synthase (NADH) large subunit. | TIGR00255 family protein. | 0.760 |
SIT70292.1 | SIT72653.1 | SAMN05216526_1280 | SAMN05216526_1702 | Glutamate synthase (NADH) large subunit. | Coproporphyrinogen III oxidase, anaerobic; Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.573 |
SIT70292.1 | hemE | SAMN05216526_1280 | SAMN05216526_0915 | Glutamate synthase (NADH) large subunit. | Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | 0.799 |
SIT70292.1 | lepA | SAMN05216526_1280 | SAMN05216526_0354 | Glutamate synthase (NADH) large subunit. | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.690 |
SIT70455.1 | SIT70292.1 | SAMN05216526_1317 | SAMN05216526_1280 | Coproporphyrinogen III oxidase, anaerobic; 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. | Glutamate synthase (NADH) large subunit. | 0.573 |
SIT70455.1 | SIT70459.1 | SAMN05216526_1317 | SAMN05216526_1318 | Coproporphyrinogen III oxidase, anaerobic; 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. | XTP/dITP diphosphohydrolase; 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. | 0.920 |
SIT70455.1 | SIT70468.1 | SAMN05216526_1317 | SAMN05216526_1320 | Coproporphyrinogen III oxidase, anaerobic; 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. | TIGR00255 family protein. | 0.616 |
SIT70455.1 | SIT70885.1 | SAMN05216526_1317 | SAMN05216526_1424 | Coproporphyrinogen III oxidase, anaerobic; 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. | Oxygen-dependent protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | 0.558 |
SIT70455.1 | SIT72653.1 | SAMN05216526_1317 | SAMN05216526_1702 | Coproporphyrinogen III oxidase, anaerobic; 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. | Coproporphyrinogen III oxidase, anaerobic; Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.599 |
SIT70455.1 | hemE | SAMN05216526_1317 | SAMN05216526_0915 | Coproporphyrinogen III oxidase, anaerobic; 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. | Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | 0.734 |
SIT70455.1 | hemF | SAMN05216526_1317 | SAMN05216526_1148 | Coproporphyrinogen III oxidase, anaerobic; 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. | Coproporphyrinogen oxidase; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. | 0.572 |
SIT70455.1 | lepA | SAMN05216526_1317 | SAMN05216526_0354 | Coproporphyrinogen III oxidase, anaerobic; 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. | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.698 |
SIT70455.1 | rlmN | SAMN05216526_1317 | SAMN05216526_1892 | Coproporphyrinogen III oxidase, anaerobic; 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. | 23S rRNA m(2)A-2503 methyltransferase; 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. | 0.737 |
SIT70455.1 | rph | SAMN05216526_1317 | SAMN05216526_1319 | Coproporphyrinogen III oxidase, anaerobic; 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. | RNAse PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.837 |
SIT70459.1 | SIT70292.1 | SAMN05216526_1318 | SAMN05216526_1280 | XTP/dITP diphosphohydrolase; 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. | Glutamate synthase (NADH) large subunit. | 0.642 |
SIT70459.1 | SIT70455.1 | SAMN05216526_1318 | SAMN05216526_1317 | XTP/dITP diphosphohydrolase; 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, anaerobic; 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. | 0.920 |
SIT70459.1 | SIT70468.1 | SAMN05216526_1318 | SAMN05216526_1320 | XTP/dITP diphosphohydrolase; 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. | TIGR00255 family protein. | 0.670 |
SIT70459.1 | rph | SAMN05216526_1318 | SAMN05216526_1319 | XTP/dITP diphosphohydrolase; 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. | RNAse PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.993 |