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CAZyme Information: MGYG000003712_00635

You are here: Home > Sequence: MGYG000003712_00635

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 Serratia liquefaciens
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Serratia; Serratia liquefaciens
CAZyme ID MGYG000003712_00635
CAZy Family GH13
CAZyme Description Trehalose-6-phosphate hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
566 MGYG000003712_7|CGC1 64691.51 5.0462
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003712 5062001 MAG Estonia Europe
Gene Location Start: 70497;  End: 72197  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 42 383 1.4e-183 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 21 480 1 428
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 19 564 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 13 565 1 551
trehalose-6-phosphate hydrolase; Provisional
COG0366 AmyA 1.27e-170 23 528 1 494
Glycosidase [Carbohydrate transport and metabolism].
pfam00128 Alpha-amylase 9.58e-165 42 384 1 332
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
QNQ54827.1 0.0 13 566 1 554
AKE12294.1 0.0 13 566 1 554
QIC85281.1 0.0 13 566 1 554
AYO36042.1 0.0 13 566 1 554
QHT49264.1 0.0 13 566 1 554

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5BRQ_A 5.67e-232 18 560 13 560
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 2.30e-231 18 560 13 560
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 1.42e-187 19 565 5 558
CrystalStructure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus]
5DO8_A 2.08e-186 19 560 6 548
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 1.67e-184 19 560 4 556
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
P28904 0.0 19 563 7 549
Trehalose-6-phosphate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=treC PE=1 SV=3
P39795 1.28e-233 18 564 7 557
Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2
Q9K8U9 3.53e-191 19 559 5 553
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
P29094 4.18e-190 19 559 5 554
Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
Q45101 2.47e-187 19 565 4 554
Oligo-1,6-glucosidase OS=Weizmannia coagulans OX=1398 GN=malL 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
1.000059 0.000004 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003712_00635.