Species | Brachyspira aalborgi | |||||||||||
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Lineage | Bacteria; Spirochaetota; Brachyspirae; Brachyspirales; Brachyspiraceae; Brachyspira; Brachyspira aalborgi | |||||||||||
CAZyme ID | MGYG000000502_02013 | |||||||||||
CAZy Family | GH57 | |||||||||||
CAZyme Description | Alpha-amylase 1 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2896; End: 5031 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH57 | 8 | 283 | 3.5e-66 | 0.7780678851174935 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd10793 | GH57N_TLGT_like | 2.63e-161 | 5 | 283 | 1 | 279 | N-terminal catalytic domain of 4-alpha-glucanotransferase; glycoside hydrolase family 57 (GH57). 4-alpha-glucanotransferase (TLGT, EC 2.4.1.25) plays a key role in the maltose metabolism. It catalyzes the disproportionation of amylose and the formation of large cyclic alpha-1,4-glucan (cycloamylose) from linear amylose. TLGT functions as a homodimer. Each monomer is composed of two domains, an N-terminal catalytic domain with a (beta/alpha)7 barrel fold and a C-terminal domain with a twisted beta-sandwich fold. Some family members have been designated as alpha-amylases, such as the heat-stable eubacterial amylase from Dictyoglomus thermophilum (DtAmyA) and the extremely thermostable archaeal amylase from Pyrococcus furiosus(PfAmyA). However, both of these proteins are 4-alpha-glucanotransferases. DtAmyA was shown to have transglycosylating activity and PfAmyA exhibits 4-alpha-glucanotransferase activity. |
pfam09095 | DUF1926 | 4.20e-89 | 415 | 697 | 1 | 274 | Domain of unknown function (DUF1926). Members of this family, which are found in a set of prokaryotic transferases, adopt a beta-sandwich fold, in which two layers of anti-parallel beta-sheets are arranged in a nearly parallel fashion. The exact function of this family is, as yet, unknown, however it has been proposed that they may play a role in transglycosylation reactions. |
pfam03065 | Glyco_hydro_57 | 1.78e-53 | 7 | 270 | 1 | 293 | Glycosyl hydrolase family 57. This family includes alpha-amylase (EC:3.2.1.1), 4--glucanotransferase (EC:2.4.1.-) and amylopullulanase enzymes. |
cd01022 | GH57N_like | 1.57e-44 | 11 | 274 | 5 | 302 | N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57. Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation. |
cd10796 | GH57N_APU | 7.49e-30 | 11 | 281 | 6 | 312 | N-terminal catalytic domain of thermoactive amylopullulanases; glycoside hydrolase family 57 (GH57). Pullulanases (EC 3.2.1.41) are capable of hydrolyzing the alpha-1,6 glucosidic bonds of pullulan, producing maltotriose. Amylopullulanases (APU, E.C 3.2.1.1/41) are type II pullulanases which can also degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch, producing oligosaccharides. This subfamily includes GH57 archaeal thermoactive APUs, which show both pullulanolytic and amylolytic activities. They have an acid pH optimum and the presence of Ca2+ might increase their activity, thermostability, and substrate affinity. Besides GH57 thermoactive APUs, all mesophilic and some thermoactive APUs belong to glycoside hydrolase family 13 with catalytic features distinct from GH57. This subfamily also includes many uncharacterized proteins found in bacteria and archaea. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AEM22783.1 | 0.0 | 1 | 711 | 1 | 706 |
QTM05487.1 | 0.0 | 1 | 711 | 1 | 706 |
ANN64255.1 | 0.0 | 1 | 711 | 1 | 706 |
ACN83624.1 | 0.0 | 1 | 711 | 1 | 706 |
AUJ49357.1 | 0.0 | 1 | 711 | 1 | 706 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1K1X_A | 5.00e-140 | 1 | 536 | 1 | 513 | Crystalstructure of 4-alpha-glucanotransferase from thermococcus litoralis [Thermococcus litoralis],1K1X_B Crystal structure of 4-alpha-glucanotransferase from thermococcus litoralis [Thermococcus litoralis],1K1Y_A Crystal structure of thermococcus litoralis 4-alpha-glucanotransferase complexed with acarbose [Thermococcus litoralis],1K1Y_B Crystal structure of thermococcus litoralis 4-alpha-glucanotransferase complexed with acarbose [Thermococcus litoralis] |
1K1W_A | 4.14e-135 | 2 | 536 | 2 | 513 | Crystalstructure of 4-alpha-glucanotransferase from thermococcus litoralis [Thermococcus litoralis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P09961 | 3.19e-155 | 2 | 694 | 3 | 671 | Alpha-amylase 1 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyA PE=1 SV=2 |
Q9V298 | 7.83e-141 | 1 | 628 | 1 | 594 | Alpha-amylase OS=Pyrococcus abyssi (strain GE5 / Orsay) OX=272844 GN=amyA PE=3 SV=1 |
O32450 | 1.15e-139 | 1 | 627 | 1 | 593 | 4-alpha-glucanotransferase OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1809 PE=3 SV=1 |
O32462 | 2.74e-139 | 1 | 536 | 1 | 513 | 4-alpha-glucanotransferase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=jgt PE=1 SV=1 |
P49067 | 5.75e-132 | 4 | 673 | 5 | 615 | Alpha-amylase OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=amyA PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000052 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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