| 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 | 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 | acpP1 | ZOBELLIA_297 | ZOBELLIA_1590 | 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. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.553 |
| CAZ94370.1 | glpE1 | ZOBELLIA_297 | ZOBELLIA_664 | 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. | Thiosulfate sulfurtransferase catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide; The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate; Contains one only rhodanese domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.589 |
| 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 | 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 | acpP1 | ZOBELLIA_384 | ZOBELLIA_1590 | 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. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.439 |
| CAZ94457.1 | glpE1 | ZOBELLIA_384 | ZOBELLIA_664 | 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. | Thiosulfate sulfurtransferase catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide; The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate; Contains one only rhodanese domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.426 |
| CAZ94457.1 | glpE4 | ZOBELLIA_384 | ZOBELLIA_1202 | 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. | Thiosulfate sulfurtransferase catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide; The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate; Contains one only rhodanese domain; Signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space; High confidence in function and specificity. | 0.426 |
| CAZ94729.1 | glpE1 | ZOBELLIA_663 | ZOBELLIA_664 | Conserved hypothetical protein; Localized in the cytoplasm. | Thiosulfate sulfurtransferase catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide; The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate; Contains one only rhodanese domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.496 |
| CAZ94731.1 | CAZ94732.1 | ZOBELLIA_665 | ZOBELLIA_666 | The transcriptional regulators with the marR-type HTH domain control a variety of biological functions, including resistance to multiple antibiotics, household disinfectants, organic solvents, oxidative stress agents. Many of the marR-like regulators respond to aromatic compounds; Contains a DNA-binding, winged helix-turn-helix (wHTH) domain; Localized in the cytoplasm; Family membership. | Conserved hypothetical protein that belongts to the YceI like family; Signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space; Belongs to the UPF0312 family. | 0.687 |
| CAZ94731.1 | glpE1 | ZOBELLIA_665 | ZOBELLIA_664 | The transcriptional regulators with the marR-type HTH domain control a variety of biological functions, including resistance to multiple antibiotics, household disinfectants, organic solvents, oxidative stress agents. Many of the marR-like regulators respond to aromatic compounds; Contains a DNA-binding, winged helix-turn-helix (wHTH) domain; Localized in the cytoplasm; Family membership. | Thiosulfate sulfurtransferase catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide; The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate; Contains one only rhodanese domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.533 |
| CAZ94732.1 | CAZ94731.1 | ZOBELLIA_666 | ZOBELLIA_665 | Conserved hypothetical protein that belongts to the YceI like family; Signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space; Belongs to the UPF0312 family. | The transcriptional regulators with the marR-type HTH domain control a variety of biological functions, including resistance to multiple antibiotics, household disinfectants, organic solvents, oxidative stress agents. Many of the marR-like regulators respond to aromatic compounds; Contains a DNA-binding, winged helix-turn-helix (wHTH) domain; Localized in the cytoplasm; Family membership. | 0.687 |
| CAZ94732.1 | glpE1 | ZOBELLIA_666 | ZOBELLIA_664 | Conserved hypothetical protein that belongts to the YceI like family; Signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space; Belongs to the UPF0312 family. | Thiosulfate sulfurtransferase catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide; The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate; Contains one only rhodanese domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.435 |
| 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 | CAZ94457.1 | ZOBELLIA_2597 | ZOBELLIA_384 | 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. | 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 |
| 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 |