EC Number | Cloned (Comment) | Organism |
---|---|---|
5.1.3.2 | expression in Escherichia coli | Bacillus anthracis |
5.1.3.2 | gene BAS5114, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3) | Bacillus anthracis |
5.1.3.7 | expression in Escherichia coli | Bacillus anthracis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
5.1.3.2 | Mg2+ | - |
Bacillus anthracis | |
5.1.3.2 | Mg2+ | 4 mM are included in assay medium | Bacillus anthracis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 36900 | - |
predicted by amino acid sequence | Bacillus anthracis |
5.1.3.2 | 37800 | - |
predicted by amino acid sequence | Bacillus anthracis |
5.1.3.7 | 37800 | - |
predicted by amino acid sequence | Bacillus anthracis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.3.2 | additional information | Bacillus anthracis | the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase | ? | - |
? | |
5.1.3.2 | additional information | Bacillus anthracis | UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview | ? | - |
? | |
5.1.3.2 | UDP-alpha-D-glucose | Bacillus anthracis | - |
UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-galactose | Bacillus anthracis | - |
UDP-glucose | - |
r | |
5.1.3.7 | additional information | Bacillus anthracis | the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase | ? | - |
? | |
5.1.3.7 | UDP-N-acetylgalactosamine | Bacillus anthracis | - |
UDP-N-acetylglucosamine | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.3.2 | Bacillus anthracis | Q81JK4 | - |
- |
5.1.3.2 | Bacillus anthracis | Q81K34 | - |
- |
5.1.3.7 | Bacillus anthracis | Q81JK4 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
5.1.3.2 | by using nickel-nitrilotriacetic acid affinity chromatography and gel filtration | Bacillus anthracis |
5.1.3.2 | recombinant enzyme from Escherichia coli strain BL21(DE3) | Bacillus anthracis |
5.1.3.7 | by using nickel-nitrilotriacetic acid affinity chromatography and gel filtration | Bacillus anthracis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.3.2 | additional information | the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase | Bacillus anthracis | ? | - |
? | |
5.1.3.2 | additional information | UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview | Bacillus anthracis | ? | - |
? | |
5.1.3.2 | additional information | no activity with UDP-N-acetylgalactoseamine | Bacillus anthracis | ? | - |
? | |
5.1.3.2 | UDP-alpha-D-glucose | - |
Bacillus anthracis | UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-galactose | - |
Bacillus anthracis | UDP-glucose | - |
r | |
5.1.3.7 | additional information | the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase | Bacillus anthracis | ? | - |
? | |
5.1.3.7 | UDP-N-acetylgalactosamine | - |
Bacillus anthracis | UDP-N-acetylglucosamine | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.1.3.2 | UDP-Glc 4-epimerase | - |
Bacillus anthracis |
5.1.3.2 | UDP-GlcNAc 4-epimerase | - |
Bacillus anthracis |
5.1.3.2 | UDP-glucose 4-epimerase | - |
Bacillus anthracis |
5.1.3.7 | UDP-N-acetylglucosamine 4-epimerase | - |
Bacillus anthracis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 37 | - |
assay at | Bacillus anthracis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 100 | - |
5 min, purified recombinant enzyme, inactivation | Bacillus anthracis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 8 | - |
assay at | Bacillus anthracis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
5.1.3.2 | additional information | contains an NAD+ binding site | Bacillus anthracis | |
5.1.3.2 | NAD+ | - |
Bacillus anthracis |
EC Number | Organism | Comment | Expression |
---|---|---|---|
5.1.3.7 | Bacillus anthracis | spores produced by a mutant strain lacking the enzyme still contain normal levels of BclA-attached oligosaccharides, monosaccharide analysis of the oligosaccharides reveals that N-acetylglucosamine had replaced N-acetylgalactosamine, significant levels of gene transcripts are detected only during sporulation, an observation consistent with a role for this gene in exosporium assembly, gene expression during sporulation appears to be biphasic | additional information |
EC Number | General Information | Comment | Organism |
---|---|---|---|
5.1.3.7 | physiological function | the epimerase is required to produce N-acetyl-galactosamine for BclA oligosaccharide biosynthesis, a collagen-like glycoprotein, UDP-GlcNAc 4-epimerase encoded by the BAS5304 gene is required for the synthesis of GalNAc in sporulating cells and that GlcNAc can replace GalNAc in the synthesis of BclA oligosaccharides | Bacillus anthracis |