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Literature summary for 2.4.1.25 extracted from
- A putative novel starch-binding domain revealed by in silico analysis of the N-terminal domain in bacterial amylomaltases from the family GH77 (2021), 3 Biotech, 11, 229.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene B9H00_13155, DNA and amino acid sequence determmination and analysis, phylogenetic analysis and tree | Kushneria marisflavi |
| gene malQ, DNA and amino acid sequence determmination and analysis, phylogenetic analysis and tree | Corynebacterium glutamicum |
| gene malQ, DNA and amino acid sequence determmination and analysis, phylogenetic analysis and tree | Escherichia coli |
| gene malQ, DNA and amino acid sequence determmination and analysis, phylogenetic analysis and tree | Pelotomaculum thermopropionicum |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis, PDB ID 4S3Q (4S3R) | Escherichia coli |
| crystal structure analysis, PDB ID 5B68 | Corynebacterium glutamicum |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | the enzyme contains a TIM barrel structure | Escherichia coli | 16020 | - |
| membrane | the enzyme contains a TIM barrel structure | Corynebacterium glutamicum | 16020 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium glutamicum | Q8NNA7 | - |
- |
| Corynebacterium glutamicum 534 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum ATCC 13032 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum BCRC 11384 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum CCUG 27702 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum DSM 20300 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum JCM 1318 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum LMG 3730 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum NBRC 12168 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum NCIMB 10025 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum NRRL B-2784 | Q8NNA7 | - |
- |
| Escherichia coli | P15977 | - |
- |
| Escherichia coli K12 | P15977 | - |
- |
| Kushneria marisflavi | A0A240US28 | - |
- |
| Pelotomaculum thermopropionicum | A5D1W1 | - |
- |
| Pelotomaculum thermopropionicum DSM 13744 | A5D1W1 | - |
- |
| Pelotomaculum thermopropionicum JCM 10971 | A5D1W1 | - |
- |
| Pelotomaculum thermopropionicum SI | A5D1W1 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Escherichia coli | ? | - |
- |
 |
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Kushneria marisflavi | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Pelotomaculum thermopropionicum | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum ATCC 13032 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Pelotomaculum thermopropionicum SI | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum DSM 20300 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Escherichia coli K12 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum JCM 1318 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum LMG 3730 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum NCIMB 10025 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum BCRC 11384 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum CCUG 27702 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum NBRC 12168 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum NRRL B-2784 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Corynebacterium glutamicum 534 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Pelotomaculum thermopropionicum DSM 13744 | ? | - |
- |
|
| additional information | maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview | Pelotomaculum thermopropionicum JCM 10971 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| additional information | the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview | Escherichia coli |
| additional information | the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview | Corynebacterium glutamicum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| amylomaltase | - |
Escherichia coli |
| amylomaltase | - |
Corynebacterium glutamicum |
| amylomaltase | - |
Kushneria marisflavi |
| amylomaltase | - |
Pelotomaculum thermopropionicum |
| B9H00_13155 | - |
Kushneria marisflavi |
| GH77 amylomaltase | - |
Escherichia coli |
| GH77 amylomaltase | - |
Corynebacterium glutamicum |
| GH77 amylomaltase | - |
Kushneria marisflavi |
| GH77 amylomaltase | - |
Pelotomaculum thermopropionicum |
| MalQ | - |
Escherichia coli |
| MalQ | - |
Corynebacterium glutamicum |
| MalQ | - |
Pelotomaculum thermopropionicum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview | Escherichia coli |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview | Corynebacterium glutamicum |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview | Kushneria marisflavi |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups. sequence comparisons, overview | Pelotomaculum thermopropionicum |
| additional information | the amylomaltase from Escherichia coli, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Residue Tyr108 may be involved in alpha-glucan binding. Molecular docking, overview | Escherichia coli |
| additional information | the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview | Corynebacterium glutamicum |
| additional information | the amylomaltase from Kushneria marisflavi, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview | Kushneria marisflavi |
| additional information | the amylomaltase from Pelotomaculum thermopropionicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview | Pelotomaculum thermopropionicum |
| physiological function | in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants | Escherichia coli |
| physiological function | in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants | Corynebacterium glutamicum |
| physiological function | in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants | Kushneria marisflavi |
| physiological function | in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants | Pelotomaculum thermopropionicum |
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