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CAZyme Information: HMPREF1541_09929-t46_1-p1

You are here: Home > Sequence: HMPREF1541_09929-t46_1-p1

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 Cyphellophora europaea
Lineage Ascomycota; Eurotiomycetes; ; Cyphellophoraceae; Cyphellophora; Cyphellophora europaea
CAZyme ID HMPREF1541_09929-t46_1-p1
CAZy Family GT32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
605 KB822713|CGC5 65352.62 4.4997
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CeuropaeaCBS101466 11153 1220924 59 11094
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 132 470 1.7e-109 0.9970760233918129

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
236518 PRK09441 2.38e-172 104 586 2 479
cytoplasmic alpha-amylase; Reviewed
200457 AmyAc_bac_fung_AmyA 7.45e-158 105 493 1 389
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.
200453 AmyAc_arch_bac_plant_AmyA 7.65e-34 108 473 2 283
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.
215419 PLN02784 5.81e-18 75 471 471 821
alpha-amylase
395077 Alpha-amylase 4.70e-17 133 472 13 330
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
2.45e-133 105 605 20 515
9.66e-129 105 604 36 532
5.98e-128 104 588 33 515
1.02e-127 105 604 12 507
8.09e-127 105 596 12 500

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.32e-121 105 588 2 483
High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens],3BH4_B High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens]
2.08e-120 105 588 2 483
Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.92A [Bacillus amyloliquefaciens],1E3Z_A Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A [Bacillus amyloliquefaciens],1E40_A Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A [Bacillus amyloliquefaciens],1E43_A Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A [Bacillus amyloliquefaciens]
7.28e-118 105 588 4 483
Structure Of Alpha-Amylase Precursor [Bacillus licheniformis]
5.75e-117 103 588 2 483
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]
2.54e-115 105 588 4 483
Bacillus Licheniformis Alpha-Amylase [Bacillus licheniformis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.18e-121 101 588 29 514
Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
3.62e-116 105 588 33 512
Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
2.03e-110 104 588 38 518
Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
5.06e-110 105 586 39 515
Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
8.86e-94 105 589 3 493
Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999162 0.000863

TMHMM  Annotations      download full data without filtering help

Start End
32 54