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CAZyme Information: MGYG000000589_01940
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; | |||||||||||
| CAZyme ID | MGYG000000589_01940 | |||||||||||
| CAZy Family | GH13 | |||||||||||
| CAZyme Description | Amylosucrase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1826; End: 2572 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd11324 | AmyAc_Amylosucrase | 1.12e-89 | 2 | 173 | 364 | 535 | 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. |
| pfam16657 | Malt_amylase_C | 0.006 | 182 | 243 | 6 | 73 | Maltogenic Amylase, C-terminal domain. This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyzes starch material. Maltogenic amylases are central to carbohydrate metabolism. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ATL90312.1 | 3.75e-179 | 1 | 247 | 361 | 607 |
| ATP00062.1 | 4.32e-178 | 1 | 247 | 361 | 607 |
| QIA44210.1 | 4.32e-178 | 1 | 247 | 361 | 607 |
| AXB28048.1 | 1.23e-177 | 1 | 247 | 361 | 607 |
| CBK98444.1 | 9.38e-177 | 1 | 247 | 359 | 605 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7ESH_A | 2.65e-40 | 3 | 246 | 392 | 644 | ChainA, amylosucrase [Calidithermus timidus DSM 17022],7ESH_B Chain B, amylosucrase [Calidithermus timidus DSM 17022],7ESH_C Chain C, amylosucrase [Calidithermus timidus DSM 17022],7ESH_D Chain D, amylosucrase [Calidithermus timidus DSM 17022] |
| 4AYS_A | 1.47e-37 | 3 | 244 | 387 | 642 | TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans] |
| 3UCQ_A | 1.40e-36 | 3 | 244 | 396 | 646 | 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] |
| 5N7J_A | 6.13e-33 | 1 | 244 | 386 | 623 | Crystalstructure of Neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides [Neisseria polysaccharea] |
| 1MVY_A | 1.57e-32 | 1 | 244 | 386 | 623 | ChainA, amylosucrase [Neisseria polysaccharea],1MW0_A Chain A, amylosucrase [Neisseria polysaccharea],1S46_A Chain A, amylosucrase [Neisseria polysaccharea],1ZS2_A Chain A, amylosucrase [Neisseria polysaccharea] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9ZEU2 | 8.88e-32 | 1 | 244 | 394 | 631 | Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1 |
| Q84HD6 | 6.19e-29 | 1 | 244 | 394 | 631 | Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000060 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |