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CAZyme Information: KIW03205.1

You are here: Home > Sequence: KIW03205.1

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 Verruconis gallopava
Lineage Ascomycota; Dothideomycetes; ; Sympoventuriaceae; Verruconis; Verruconis gallopava
CAZyme ID KIW03205.1
CAZy Family GH28
CAZyme Description Aamy domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0D2A9D6]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
594 KN847545|CGC4 69034.76 5.8529
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_VgallopavaCBS43764 9871 N/A 53 9818
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 5.4.99.11:5 3.2.1.20:4 3.2.1.10:1 3.2.1.-:1 3.2.1.70:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 34 394 1.5e-166 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 13 504 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.
200470 AmyAc_OligoGlu_like 2.88e-155 10 504 1 442
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, 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. 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 (Asp, Glu and Asp) 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.
182849 PRK10933 2.90e-148 9 589 5 546
trehalose-6-phosphate hydrolase; Provisional
200469 AmyAc_OligoGlu 3.11e-148 11 504 2 453
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, 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. 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 (Asp, Glu and Asp) 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.
223443 AmyA 2.21e-132 15 563 1 501
Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.36e-299 1 591 1 589
8.19e-266 10 591 11 596
2.34e-265 10 591 11 596
5.05e-265 11 591 17 598
1.91e-264 10 591 11 596

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.04e-163 11 590 5 554
Crystal Structure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus]
2.29e-162 7 588 10 583
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]
1.83e-161 7 588 10 583
Crystal structure of isomaltase in complex with isomaltose [Saccharomyces cerevisiae],3AXI_A Crystal structure of isomaltase in complex with maltose [Saccharomyces cerevisiae]
5.86e-159 10 590 15 577
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]
2.12e-149 9 587 3 550
Crystal structure of the isomaltulose synthase SmuA from Protaminobacter rubrum [Serratia plymuthica],3GBE_A Crystal structure of the isomaltulose synthase SmuA from Protaminobacter rubrum in complex with the inhibitor deoxynojirimycin [Serratia plymuthica]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.83e-192 9 590 11 576
Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mal1 PE=2 SV=1
1.08e-171 11 587 5 553
Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
1.83e-163 7 588 10 583
Oligo-1,6-glucosidase IMA2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA2 PE=2 SV=1
5.35e-163 11 590 5 554
Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
1.18e-161 7 588 10 583
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
1.000046 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KIW03205.1.