logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: QHS74051.1

You are here: Home > Sequence: QHS74051.1

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 Saccharomyces paradoxus
Lineage Ascomycota; Saccharomycetes; ; Saccharomycetaceae; Saccharomyces; Saccharomyces paradoxus
CAZyme ID QHS74051.1
CAZy Family GH72
CAZyme Description Ima3
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
589 CP020251|CGC2 68503.56 5.2002
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_SparadoxusCBS432 5803 N/A 275 5528
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.10:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 37 399 2.1e-188 0.9972144846796658

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
200472 AmyAc_SI_OligoGlu_DGase 0.0 16 503 1 427
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.
274115 trehalose_treC 3.40e-172 14 587 1 542
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.
395077 Alpha-amylase 8.20e-160 37 400 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.
182849 PRK10933 4.82e-143 10 589 3 551
trehalose-6-phosphate hydrolase; Provisional
223443 AmyA 2.67e-142 18 555 1 495
Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 589 1 589
0.0 1 589 1 589
0.0 1 589 1 589
0.0 1 589 1 589
0.0 1 589 1 589

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 1 589 1 589
Crystal structure of isomaltase in complex with isomaltose [Saccharomyces cerevisiae],3AXI_A Crystal structure of isomaltase in complex with maltose [Saccharomyces cerevisiae]
0.0 1 589 1 589
Crystal structure of isomaltase from Saccharomyces cerevisiae [Saccharomyces cerevisiae],3A4A_A Crystal structure of isomaltase from Saccharomyces cerevisiae [Saccharomyces cerevisiae],3AJ7_A Crystal Structure of isomaltase from Saccharomyces cerevisiae [Saccharomyces cerevisiae]
6.12e-179 9 586 11 578
Chain A, BaAG2 [Blastobotrys adeninivorans],7P01_B Chain B, BaAG2 [Blastobotrys adeninivorans],7P07_A Chain A, BaAG2 [Blastobotrys adeninivorans],7P07_B Chain B, BaAG2 [Blastobotrys adeninivorans]
1.29e-158 13 588 3 560
The Structure 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]
1.83e-158 13 588 3 560
The Structure of MalL mutant enzyme G202P from Bacillus subtilus [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
0.0 1 587 1 582
Alpha-glucosidase MAL12 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MAL12 PE=1 SV=1
0.0 1 589 1 589
Oligo-1,6-glucosidase IMA4 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA4 PE=3 SV=1
0.0 1 587 1 582
Alpha-glucosidase MAL32 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MAL32 PE=1 SV=1
0.0 1 589 1 589
Oligo-1,6-glucosidase IMA3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA3 PE=1 SV=1
0.0 1 589 1 589
Oligo-1,6-glucosidase IMA1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000072 0.000005

TMHMM  Annotations      help

There is no transmembrane helices in QHS74051.1.