dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Coprinopsis cinerea

Lineage

Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea

CAZyme ID

KAG2024049.1

CAZy Family

PL4

CAZyme Description

alpha amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
326		38012.74	5.4863

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccinerea326	15250	N/A	238	15012

Gene Location

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	1	132	2.8e-42	0.35376044568245124

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200472	AmyAc_SI_OligoGlu_DGase	1.43e-80	1	237	245	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.
182849	PRK10933	1.03e-57	1	322	247	546	trehalose-6-phosphate hydrolase; Provisional
223443	AmyA	1.94e-35	1	282	241	491	Glycosidase [Carbohydrate transport and metabolism].
200469	AmyAc_OligoGlu	2.25e-29	1	251	261	469	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.
395077	Alpha-amylase	1.35e-26	1	133	210	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
9.09e-126	1	320	269	587
8.87e-82	2	320	267	599
1.25e-81	2	281	267	562
1.75e-81	2	320	267	599
1.55e-75	2	300	260	559

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.94e-58	22	321	270	552	The crystal structure of isomaltulose synthase mutant E295A from Erwinia rhapontici NX5 in complex with D-glucose [Erwinia rhapontici]
1.94e-58	22	321	270	552	The crystal structure of isomaltulose synthase from Erwinia rhapontici NX5 in complex with Tris [Erwinia rhapontici]
1.94e-58	22	321	270	552	The crystal structure of isomaltulose synthase mutant D241A from Erwinia rhapontici NX5 in complex with D-glucose [Erwinia rhapontici]
1.94e-58	22	321	270	552	The crystal structure of isomaltulose synthase mutant E295Q from Erwinia rhapontici NX5 in complex with its natural substrate sucrose [Erwinia rhapontici]
4.01e-58	22	321	311	593	The crystal structure of isomaltulose synthase from Erwinia rhapontici NX5 [Erwinia rhapontici]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.06e-69	2	322	266	575	Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mal1 PE=2 SV=1
2.98e-63	1	321	252	554	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
2.29e-58	1	283	259	538	Alpha-glucosidase OS=Candida albicans OX=5476 GN=MAL2 PE=1 SV=4
3.75e-57	1	324	251	555	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
1.62e-54	1	303	251	538	Probable oligo-1,6-glucosidase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=ycdG PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000066	0.000000

TMHMM Annotations help

There is no transmembrane helices in KAG2024049.1.

You are here: Home > Sequence: KAG2024049.1