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CAZyme Information: MGYG000003534_00408

You are here: Home > Sequence: MGYG000003534_00408

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 Treponema_D sp900769325
Lineage Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900769325
CAZyme ID MGYG000003534_00408
CAZy Family GH57
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
664 76242.96 6.995
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003534 2560433 MAG Fiji Oceania
Gene Location Start: 7105;  End: 9099  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003534_00408.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH57 23 367 1.5e-35 0.9295039164490861

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10793 GH57N_TLGT_like 5.30e-30 22 279 18 277
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 1.14e-16 26 268 51 293
Glycosyl hydrolase family 57. This family includes alpha-amylase (EC:3.2.1.1), 4--glucanotransferase (EC:2.4.1.-) and amylopullulanase enzymes.
pfam09095 DUF1926 3.24e-07 388 542 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.
cd01022 GH57N_like 3.78e-06 36 272 41 301
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.
cd10798 GH57N_like_1 6.20e-05 46 153 65 190
Uncharacterized subfamily of glycoside hydrolase family 57 (GH57). This subfamily of uncharacterized bacterial proteins, shows high sequence homology to glycoside hydrolase family 57 (GH57). 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).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNL97410.1 5.06e-205 19 664 18 665
QTQ16225.1 5.24e-188 26 663 26 656
QTQ11807.1 7.41e-188 26 663 26 656
QSI02287.1 1.45e-186 1 658 1 656
QTQ14015.1 1.91e-185 26 663 26 656

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1K1X_A 6.95e-27 1 433 1 438
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 1.94e-23 24 433 24 438
Crystalstructure of 4-alpha-glucanotransferase from thermococcus litoralis [Thermococcus litoralis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P09961 4.44e-31 23 436 24 453
Alpha-amylase 1 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyA PE=1 SV=2
P49067 2.76e-26 24 563 25 588
Alpha-amylase OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=amyA PE=1 SV=2
O32462 3.80e-26 1 433 1 438
4-alpha-glucanotransferase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=jgt PE=1 SV=1
Q9V298 1.14e-24 23 563 23 596
Alpha-amylase OS=Pyrococcus abyssi (strain GE5 / Orsay) OX=272844 GN=amyA PE=3 SV=1
O57932 4.20e-23 23 473 23 492
Alpha-amylase OS=Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) OX=70601 GN=amyA 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
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003534_00408.