| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ94370.1 | CAZ96747.1 | ZOBELLIA_297 | ZOBELLIA_2597 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | 0.953 |
| CAZ94370.1 | CAZ98563.1 | ZOBELLIA_297 | ZOBELLIA_4428 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.960 |
| CAZ94370.1 | mraW | ZOBELLIA_297 | ZOBELLIA_801 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | 0.877 |
| CAZ96747.1 | CAZ94370.1 | ZOBELLIA_2597 | ZOBELLIA_297 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.953 |
| CAZ96747.1 | CAZ98563.1 | ZOBELLIA_2597 | ZOBELLIA_4428 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.959 |
| CAZ96747.1 | mraW | ZOBELLIA_2597 | ZOBELLIA_801 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | 0.877 |
| CAZ98563.1 | CAZ94370.1 | ZOBELLIA_4428 | ZOBELLIA_297 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.960 |
| CAZ98563.1 | CAZ96747.1 | ZOBELLIA_4428 | ZOBELLIA_2597 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | 0.959 |
| CAZ98563.1 | mraW | ZOBELLIA_4428 | ZOBELLIA_801 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | 0.877 |
| ftsA | ftsI | ZOBELLIA_791 | ZOBELLIA_799 | Cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family. | Peptidoglycan synthetase, family GT51; Enzyme essential for the formation of a septum of the murein sacculus. Synthetizes the cross-linked peptidoglycan from the lipid intermediates; Contains in its N-terminal half part a transmembrane segment and an penicillin insensitive transglycosylase domain (formation of linear glycan strands). In its C-terminal half part, a penicillin- sensitive transpeptidase domain (cross-linking of the peptide subunits) and a PASTA domain that binds the beta-lactam stem are present; Belongs to the family 51 of glycosyl transferases (GT51); Except for the cyto [...] | 0.906 |
| ftsA | mraW | ZOBELLIA_791 | ZOBELLIA_801 | Cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family. | S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | 0.815 |
| ftsA | mraZ | ZOBELLIA_791 | ZOBELLIA_802 | Cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family. | Protein that could play a role in cell-wall biosynthesis and/or cell division. However, to date, there has been no clear functional assignment provided for MraZ protein. MraZ is a homooctamer or homododecamer to forms a ring; Localized in the cytoplasm; Function unclear. | 0.803 |
| ftsA | murE | ZOBELLIA_791 | ZOBELLIA_798 | Cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family. | UDP-N-acetylmuramoylalanyl-D-glutamate-2, 6-diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily. | 0.893 |
| ftsI | ftsA | ZOBELLIA_799 | ZOBELLIA_791 | Peptidoglycan synthetase, family GT51; Enzyme essential for the formation of a septum of the murein sacculus. Synthetizes the cross-linked peptidoglycan from the lipid intermediates; Contains in its N-terminal half part a transmembrane segment and an penicillin insensitive transglycosylase domain (formation of linear glycan strands). In its C-terminal half part, a penicillin- sensitive transpeptidase domain (cross-linking of the peptide subunits) and a PASTA domain that binds the beta-lactam stem are present; Belongs to the family 51 of glycosyl transferases (GT51); Except for the cyto [...] | Cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family. | 0.906 |
| ftsI | mraW | ZOBELLIA_799 | ZOBELLIA_801 | Peptidoglycan synthetase, family GT51; Enzyme essential for the formation of a septum of the murein sacculus. Synthetizes the cross-linked peptidoglycan from the lipid intermediates; Contains in its N-terminal half part a transmembrane segment and an penicillin insensitive transglycosylase domain (formation of linear glycan strands). In its C-terminal half part, a penicillin- sensitive transpeptidase domain (cross-linking of the peptide subunits) and a PASTA domain that binds the beta-lactam stem are present; Belongs to the family 51 of glycosyl transferases (GT51); Except for the cyto [...] | S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | 0.880 |
| ftsI | mraZ | ZOBELLIA_799 | ZOBELLIA_802 | Peptidoglycan synthetase, family GT51; Enzyme essential for the formation of a septum of the murein sacculus. Synthetizes the cross-linked peptidoglycan from the lipid intermediates; Contains in its N-terminal half part a transmembrane segment and an penicillin insensitive transglycosylase domain (formation of linear glycan strands). In its C-terminal half part, a penicillin- sensitive transpeptidase domain (cross-linking of the peptide subunits) and a PASTA domain that binds the beta-lactam stem are present; Belongs to the family 51 of glycosyl transferases (GT51); Except for the cyto [...] | Protein that could play a role in cell-wall biosynthesis and/or cell division. However, to date, there has been no clear functional assignment provided for MraZ protein. MraZ is a homooctamer or homododecamer to forms a ring; Localized in the cytoplasm; Function unclear. | 0.859 |
| ftsI | murE | ZOBELLIA_799 | ZOBELLIA_798 | Peptidoglycan synthetase, family GT51; Enzyme essential for the formation of a septum of the murein sacculus. Synthetizes the cross-linked peptidoglycan from the lipid intermediates; Contains in its N-terminal half part a transmembrane segment and an penicillin insensitive transglycosylase domain (formation of linear glycan strands). In its C-terminal half part, a penicillin- sensitive transpeptidase domain (cross-linking of the peptide subunits) and a PASTA domain that binds the beta-lactam stem are present; Belongs to the family 51 of glycosyl transferases (GT51); Except for the cyto [...] | UDP-N-acetylmuramoylalanyl-D-glutamate-2, 6-diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily. | 0.973 |
| mraW | CAZ94370.1 | ZOBELLIA_801 | ZOBELLIA_297 | S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.877 |
| mraW | CAZ96747.1 | ZOBELLIA_801 | ZOBELLIA_2597 | S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | 0.877 |
| mraW | CAZ98563.1 | ZOBELLIA_801 | ZOBELLIA_4428 | S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.877 |