Species | Treponema_D sp900541995 | |||||||||||
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Lineage | Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900541995 | |||||||||||
CAZyme ID | MGYG000000479_00977 | |||||||||||
CAZy Family | GH57 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 36795; End: 38780 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH57 | 25 | 352 | 7e-38 | 0.8903394255874674 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd10793 | GH57N_TLGT_like | 2.60e-42 | 20 | 211 | 16 | 214 | 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. |
pfam03065 | Glyco_hydro_57 | 1.85e-18 | 23 | 208 | 40 | 242 | 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 | 1.22e-12 | 24 | 222 | 22 | 252 | 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. |
pfam09095 | DUF1926 | 2.52e-10 | 390 | 545 | 1 | 188 | 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. |
cd10795 | GH57N_MJA1_like | 1.71e-05 | 13 | 117 | 31 | 137 | N-terminal catalytic domain of a thermoactive alpha-amylase from Methanococcus jannaschii and similar proteins; glycoside hydrolase family 57 (GH57). The subfamily is represented by a thermostable alpha-amylase (MJA1, EC 3.2.1.1) encoded from the hyperthermophilic archaeon Methanococcus jannaschii locus, M J1611. MJA1 has a broad pH optimum 5.0-8.0. It exhibits extremely thermophilic alpha-amylase activity that catalyzes the hydrolysis of large sugar polymers with alpha-l,6 and alpha-l,4 linkages, and yields products including glucose polymers of 1-7 units. MJ1611 also encodes another alpha-amylase with catalytic features distinct from MJA1, which belongs to glycoside hydrolase family 13 (GH-13), and is not included here. This subfamily also includes many uncharacterized proteins found in bacteria and archaea. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QPZ99899.1 | 0.0 | 1 | 661 | 1 | 661 |
AEB14246.1 | 2.42e-257 | 7 | 658 | 6 | 653 |
QOS39947.1 | 2.54e-223 | 5 | 659 | 4 | 652 |
QTQ14015.1 | 2.41e-174 | 1 | 660 | 1 | 656 |
QTQ11807.1 | 4.82e-174 | 1 | 660 | 1 | 656 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1K1X_A | 1.16e-15 | 23 | 178 | 23 | 181 | 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 | 2.66e-15 | 23 | 178 | 23 | 181 | Crystalstructure of 4-alpha-glucanotransferase from thermococcus litoralis [Thermococcus litoralis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P09961 | 2.38e-27 | 24 | 543 | 25 | 586 | Alpha-amylase 1 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyA PE=1 SV=2 |
O57932 | 1.11e-19 | 24 | 545 | 24 | 554 | Alpha-amylase OS=Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) OX=70601 GN=amyA PE=3 SV=1 |
O32450 | 1.03e-17 | 24 | 435 | 24 | 438 | 4-alpha-glucanotransferase OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1809 PE=3 SV=1 |
P49067 | 7.21e-17 | 23 | 545 | 24 | 567 | Alpha-amylase OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=amyA PE=1 SV=2 |
Q9V298 | 6.78e-16 | 24 | 545 | 24 | 575 | Alpha-amylase OS=Pyrococcus abyssi (strain GE5 / Orsay) OX=272844 GN=amyA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000048 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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