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CAZyme Information: MGYG000000264_02035

You are here: Home > Sequence: MGYG000000264_02035

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 Exiguobacterium sp003467445
Lineage Bacteria; Firmicutes; Bacilli; Exiguobacterales; Exiguobacteraceae; Exiguobacterium; Exiguobacterium sp003467445
CAZyme ID MGYG000000264_02035
CAZy Family GH13
CAZyme Description Alpha-amylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
514 57678.94 6.9839
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000264 2830712 Isolate China Asia
Gene Location Start: 191281;  End: 192825  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.1 3.2.1.98 3.2.1.- 3.2.1.41

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 60 400 1.9e-151 0.9970760233918129

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09441 PRK09441 0.0 31 511 1 478
cytoplasmic alpha-amylase; Reviewed
cd11318 AmyAc_bac_fung_AmyA 0.0 33 424 1 391
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.
cd11314 AmyAc_arch_bac_plant_AmyA 8.48e-53 36 398 2 276
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.
COG0366 AmyA 1.08e-26 60 510 37 441
Glycosidase [Carbohydrate transport and metabolism].
smart00642 Aamy 2.31e-24 35 197 2 163
Alpha-amylase domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUE86983.1 0.0 1 514 1 514
AFZ41193.1 0.0 1 514 1 514
QPI68042.1 0.0 1 514 1 514
ACQ70333.1 0.0 1 514 1 514
QUP87495.1 0.0 1 514 1 514

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2DIE_A 1.18e-266 33 514 6 485
Alkalinealpha-amylase AmyK from Bacillus sp. KSM-1378 [Bacillus sp. (in: Bacteria)]
6TOY_A 1.48e-264 33 514 4 483
Crystalstructure 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]
1E3X_A 1.48e-264 33 514 2 483
Nativestructure 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]
1VJS_A 1.21e-263 33 514 4 483
StructureOf Alpha-Amylase Precursor [Bacillus licheniformis]
3BH4_A 3.47e-263 33 514 2 483
Highresolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens],3BH4_B High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P06278 1.66e-263 26 514 26 512
Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P00692 2.95e-262 3 514 4 514
Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P19571 5.33e-259 33 514 39 518
Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P06279 6.06e-242 5 511 9 514
Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P26613 1.67e-126 32 511 2 489
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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000429 0.998667 0.000204 0.000290 0.000222 0.000188

TMHMM  Annotations      download full data without filtering help

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