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CAZyme Information: EAQ90386.1

You are here: Home > Sequence: EAQ90386.1

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 Chaetomium globosum
Lineage Ascomycota; Sordariomycetes; ; Chaetomiaceae; Chaetomium; Chaetomium globosum
CAZyme ID EAQ90386.1
CAZy Family GH55
CAZyme Description Aamy domain-containing protein [Source:UniProtKB/TrEMBL;Acc:Q2HBT3]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
529 CH408030|CGC16 59799.87 4.9824
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CglobosumCBS148.51 11232 306901 184 11048
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.1:2 3.2.1.116:1 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 85 402 3.1e-108 0.9064327485380117

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
200457 AmyAc_bac_fung_AmyA 6.45e-174 57 401 1 338
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes bacterial and fungal proteins. 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.
236518 PRK09441 1.43e-160 56 490 2 479
cytoplasmic alpha-amylase; Reviewed
200453 AmyAc_arch_bac_plant_AmyA 1.06e-30 60 401 2 247
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. 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.
214758 Aamy 9.31e-16 58 161 1 97
Alpha-amylase domain.
215419 PLN02784 3.21e-15 58 396 503 786
alpha-amylase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.76e-211 82 503 1 468
2.20e-206 1 511 1 581
4.12e-195 1 503 1 558
3.26e-166 81 503 1 465
6.30e-162 50 503 38 540

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.78e-110 57 490 4 481
Crystal structure of Bacillus paralicheniformis wild-type alpha-amylase [Bacillus licheniformis],6TOZ_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with acarbose [Bacillus licheniformis],6TP0_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with maltose [Bacillus licheniformis],6TP1_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with maltotetraose [Bacillus licheniformis],6TP2_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with beta-cyclodextrin [Bacillus licheniformis]
8.74e-110 57 491 4 479
Crystal structure of calcium-free alpha-amylase from Bacillus sp. strain KSM-K38 (AmyK38) [Bacillus sp. KSM-K38],1UD4_A Crystal structure of calcium free alpha amylase from Bacillus sp. strain KSM-K38 (AmyK38, in calcium containing solution) [Bacillus sp. KSM-K38],1UD5_A Crystal structure of AmyK38 with rubidium ion [Bacillus sp. KSM-K38],1UD6_A Crystal structure of AmyK38 with potassium ion [Bacillus sp. KSM-K38],1UD8_A Crystal structure of AmyK38 with lithium ion [Bacillus sp. KSM-K38]
8.74e-110 57 491 4 479
Chain A, amylase [Bacillus sp. KSM-K38]
3.80e-109 57 490 4 481
Structure Of Alpha-Amylase Precursor [Bacillus licheniformis]
5.98e-108 57 490 4 481
Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface [Bacillus licheniformis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.34e-108 57 490 33 510
Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
1.30e-101 57 490 33 512
Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
4.23e-99 57 490 39 515
Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
1.53e-97 56 491 38 517
Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
6.65e-76 55 490 1 490
Cytoplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=amyA PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000042 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in EAQ90386.1.