| Species | Bifidobacterium breve | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium breve | |||||||||||
| CAZyme ID | MGYG000002469_00409 | |||||||||||
| CAZy Family | GH13 | |||||||||||
| CAZyme Description | Amylosucrase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 484548; End: 485000 Strand: + | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd11324 | AmyAc_Amylosucrase | 8.85e-71 | 2 | 133 | 22 | 157 | Alpha amylase catalytic domain found in Amylosucrase. Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. |
| smart00642 | Aamy | 2.50e-13 | 53 | 133 | 3 | 91 | Alpha-amylase domain. |
| cd00551 | AmyAc_family | 3.22e-12 | 55 | 133 | 18 | 97 | Alpha amylase catalytic domain family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; and C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost this catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. |
| PRK10785 | PRK10785 | 4.74e-12 | 57 | 133 | 174 | 247 | maltodextrin glucosidase; Provisional |
| COG0366 | AmyA | 6.90e-11 | 59 | 133 | 26 | 98 | Glycosidase [Carbohydrate transport and metabolism]. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ABE95061.1 | 6.23e-107 | 1 | 150 | 1 | 150 |
| QFV13670.1 | 1.76e-106 | 1 | 150 | 31 | 180 |
| AUD82405.1 | 1.79e-106 | 1 | 150 | 1 | 150 |
| AHJ15093.1 | 1.53e-103 | 1 | 150 | 44 | 193 |
| AEF27348.1 | 1.53e-103 | 1 | 150 | 44 | 193 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4AYS_A | 3.68e-34 | 2 | 133 | 44 | 177 | TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans] |
| 3UCQ_A | 1.33e-33 | 13 | 133 | 62 | 182 | Crystalstructure of amylosucrase from Deinococcus geothermalis [Deinococcus geothermalis DSM 11300],3UER_A Crystal structure of amylosucrase from Deinococcus geothermalis in complex with turanose [Deinococcus geothermalis DSM 11300] |
| 4FLS_A | 9.21e-31 | 2 | 133 | 49 | 184 | Crystalstructure of Amylosucrase inactive double mutant F290K-E328Q from Neisseria polysaccharea in complex with sucrose. [Neisseria polysaccharea] |
| 4FLR_A | 9.21e-31 | 2 | 133 | 49 | 184 | Crystalstructure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea [Neisseria polysaccharea] |
| 4FLQ_A | 9.21e-31 | 2 | 133 | 49 | 184 | Crystalstructure of Amylosucrase double mutant A289P-F290I from Neisseria polysaccharea. [Neisseria polysaccharea] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9ZEU2 | 5.14e-30 | 2 | 133 | 57 | 192 | Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1 |
| Q84HD6 | 1.80e-29 | 2 | 133 | 57 | 192 | Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1 |
| P0CW40 | 3.73e-09 | 36 | 139 | 9 | 115 | Oligo-1,6-glucosidase IMA3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA3 PE=1 SV=1 |
| Q08295 | 3.73e-09 | 36 | 139 | 9 | 115 | Oligo-1,6-glucosidase IMA2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA2 PE=2 SV=1 |
| P0CW41 | 3.73e-09 | 36 | 139 | 9 | 115 | Oligo-1,6-glucosidase IMA4 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA4 PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000051 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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