logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004883_00062

You are here: Home > Sequence: MGYG000004883_00062

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 Rothia mucilaginosa_B
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Rothia; Rothia mucilaginosa_B
CAZyme ID MGYG000004883_00062
CAZy Family GH13
CAZyme Description Trehalose-6-phosphate hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
609 MGYG000004883_1|CGC1 68193.15 4.4904
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004883 2241611 MAG China Asia
Gene Location Start: 74591;  End: 76420  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.93 3.2.1.20

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 49 404 3.2e-162 0.9941860465116279

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11333 AmyAc_SI_OligoGlu_DGase 0.0 29 506 2 428
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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.
TIGR02403 trehalose_treC 0.0 26 607 1 543
alpha,alpha-phosphotrehalase. Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.
PRK10933 PRK10933 0.0 31 608 12 551
trehalose-6-phosphate hydrolase; Provisional
COG0366 AmyA 4.75e-138 30 574 1 504
Glycosidase [Carbohydrate transport and metabolism].
pfam00128 Alpha-amylase 1.50e-120 49 404 1 331
Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAS19832.1 0.0 1 609 1 610
QXW99157.1 0.0 1 609 1 610
BAI65647.1 0.0 1 609 1 610
ATF62988.1 0.0 1 609 1 614
VEJ31035.1 0.0 27 608 8 614

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5BRQ_A 2.98e-177 30 576 18 541
Crystalstructure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_B Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_C Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_D Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580]
5BRP_A 1.20e-176 30 576 18 541
Crystalstructure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_B Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_C Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_D Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580]
1UOK_A 1.06e-135 30 603 9 553
CrystalStructure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus]
5DO8_A 3.43e-133 30 609 10 554
1.8Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e],5DO8_B 1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e],5DO8_C 1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e]
4M56_A 1.60e-126 30 602 8 555
TheStructure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],4M56_B The Structure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P39795 1.35e-173 30 563 12 519
Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2
P29094 2.09e-139 30 602 9 554
Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
P28904 5.88e-139 29 602 10 545
Trehalose-6-phosphate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=treC PE=1 SV=3
Q9K8U9 2.86e-136 30 602 9 553
Oligo-1,6-glucosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=malL PE=3 SV=1
P21332 5.83e-135 30 603 9 553
Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 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
0.956662 0.043068 0.000086 0.000078 0.000052 0.000079

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004883_00062.