node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ94075.1 | dnaA | ZOBELLIA_2 | ZOBELLIA_0 | Methyltransferases; Enzyme that uses S-AdoMet in the methylation of diverse substrates; Belongs to the UPF0011 family; Localized in the cytoplasm; Specificity unclear. | Chromosomal replication initiator protein, DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family. | 0.928 |
CAZ94075.1 | ptpA | ZOBELLIA_2 | ZOBELLIA_1 | Methyltransferases; Enzyme that uses S-AdoMet in the methylation of diverse substrates; Belongs to the UPF0011 family; Localized in the cytoplasm; Specificity unclear. | The low molecular weight (LMW) protein-tyrosine phosphatases (or acid phosphatases) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate; Belongs to the Tyrosine-specific protein phosphatases family; Localized in the cytoplasm; High confidence in function and specificity. | 0.930 |
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 | ptpA | ZOBELLIA_297 | ZOBELLIA_1 | 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. | The low molecular weight (LMW) protein-tyrosine phosphatases (or acid phosphatases) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate; Belongs to the Tyrosine-specific protein phosphatases family; Localized in the cytoplasm; High confidence in function and specificity. | 0.844 |
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 | ptpA | ZOBELLIA_384 | ZOBELLIA_1 | 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. | The low molecular weight (LMW) protein-tyrosine phosphatases (or acid phosphatases) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate; Belongs to the Tyrosine-specific protein phosphatases family; Localized in the cytoplasm; High confidence in function and specificity. | 0.550 |
CAZ95741.1 | ptpA | ZOBELLIA_1687 | ZOBELLIA_1 | Fructosamine kinase is responsible for the removal of fructosamines from proteins, by a sugar phosphorylation mechanism; Localized in the cytoplasm; High confidence in function and specificity. | The low molecular weight (LMW) protein-tyrosine phosphatases (or acid phosphatases) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate; Belongs to the Tyrosine-specific protein phosphatases family; Localized in the cytoplasm; High confidence in function and specificity. | 0.590 |
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 |
CAZ96747.1 | ptpA | ZOBELLIA_2597 | ZOBELLIA_1 | 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. | The low molecular weight (LMW) protein-tyrosine phosphatases (or acid phosphatases) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate; Belongs to the Tyrosine-specific protein phosphatases family; Localized in the cytoplasm; High confidence in function and specificity. | 0.844 |
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 | CAZ94457.1 | ZOBELLIA_4428 | ZOBELLIA_384 | 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. | 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 |
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 | ptpA | ZOBELLIA_4428 | ZOBELLIA_1 | 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. | The low molecular weight (LMW) protein-tyrosine phosphatases (or acid phosphatases) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate; Belongs to the Tyrosine-specific protein phosphatases family; Localized in the cytoplasm; High confidence in function and specificity. | 0.844 |
capC | etkA | ZOBELLIA_3787 | ZOBELLIA_1108 | Tyrosine-protein phosphatase; Dephosphorylates the phosphotyrosine-containing proteins required for the biosynthesis of type 1 capsular polysaccharide; Involved in the capsular polysaccharide (CPS) biosynthesis; Uses the mamganese as cofactor; Contains a polymerase and histidinol Phosphatase domain (PHP domain; Localized in the cytoplasm; High confidence in function and specificity. | Tyrosine-protein kinase; May be involved in the production and the transport of exopolysaccharides; Contains a N-terminal transmembrane segment; Belongs to the etk/wzc family; Localized in the cytoplasmic membrane; Specificity unclear. | 0.854 |