node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ94370.1 | CAZ94457.1 | ZOBELLIA_297 | ZOBELLIA_384 | 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. | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity unclear. | 0.911 |
CAZ94370.1 | CAZ95591.1 | ZOBELLIA_297 | ZOBELLIA_1535 | 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 belonging to the Glyoxalase superfamily; Localized in the cytoplasm; Family membership. | 0.909 |
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 | CAZ98106.1 | ZOBELLIA_297 | ZOBELLIA_3969 | 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. | Glyoxalase superfamily protein; Contains a signal peptide cleaved between the residues 20 and 21; Belongs to the Glyoxalase superfamily; Localized in the periplasmic space; Family membership. | 0.909 |
CAZ94370.1 | CAZ98522.1 | ZOBELLIA_297 | ZOBELLIA_4387 | 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. | Type III polyketide synthases are homodimeric enzymes that iteratively carry out the polyketide synthesis at one single active site; Belongs to the chalcone/stilbene synthase family; Localized in the cytoplasm; Specificity unclear. | 0.871 |
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 | ddh | ZOBELLIA_297 | ZOBELLIA_3868 | 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. | NAD-dependent 2-hydroxyacid dehydrogenases are enzymes which seem to be specific for the D-isomer of their substrate. these enzymes are composed of a substrate-binding domain and a NAD-binding domain (Rossman fold); Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.915 |
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 |
CAZ94370.1 | rpsQ | ZOBELLIA_297 | ZOBELLIA_2519 | 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. | Ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.907 |
CAZ94370.1 | ybeY | ZOBELLIA_297 | ZOBELLIA_1716 | 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. | Conserved hypothetical protein; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | 0.932 |
CAZ94457.1 | CAZ94370.1 | ZOBELLIA_384 | ZOBELLIA_297 | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity 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. | 0.911 |
CAZ94457.1 | CAZ96747.1 | ZOBELLIA_384 | ZOBELLIA_2597 | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity 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. | 0.911 |
CAZ94457.1 | CAZ98522.1 | ZOBELLIA_384 | ZOBELLIA_4387 | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity unclear. | Type III polyketide synthases are homodimeric enzymes that iteratively carry out the polyketide synthesis at one single active site; Belongs to the chalcone/stilbene synthase family; Localized in the cytoplasm; Specificity unclear. | 0.943 |
CAZ94457.1 | CAZ98563.1 | ZOBELLIA_384 | ZOBELLIA_4428 | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity 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. | 0.911 |
CAZ94457.1 | ddh | ZOBELLIA_384 | ZOBELLIA_3868 | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity unclear. | NAD-dependent 2-hydroxyacid dehydrogenases are enzymes which seem to be specific for the D-isomer of their substrate. these enzymes are composed of a substrate-binding domain and a NAD-binding domain (Rossman fold); Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.485 |
CAZ95591.1 | CAZ94370.1 | ZOBELLIA_1535 | ZOBELLIA_297 | Protein belonging to the Glyoxalase superfamily; Localized in the cytoplasm; Family membership. | 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. | 0.909 |
CAZ95591.1 | CAZ96747.1 | ZOBELLIA_1535 | ZOBELLIA_2597 | Protein belonging to the Glyoxalase superfamily; Localized in the cytoplasm; Family membership. | 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. | 0.909 |
CAZ95591.1 | CAZ98106.1 | ZOBELLIA_1535 | ZOBELLIA_3969 | Protein belonging to the Glyoxalase superfamily; Localized in the cytoplasm; Family membership. | Glyoxalase superfamily protein; Contains a signal peptide cleaved between the residues 20 and 21; Belongs to the Glyoxalase superfamily; Localized in the periplasmic space; Family membership. | 0.900 |
CAZ95591.1 | CAZ98563.1 | ZOBELLIA_1535 | ZOBELLIA_4428 | Protein belonging to the Glyoxalase superfamily; Localized in the cytoplasm; Family membership. | 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. | 0.909 |
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 |