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CAZyme Information: MGYG000002538_03296

You are here: Home > Sequence: MGYG000002538_03296

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 Klebsiella pneumoniae
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella pneumoniae
CAZyme ID MGYG000002538_03296
CAZy Family GH13
CAZyme Description Cytoplasmic alpha-amylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
495 MGYG000002538_1|CGC41 56250.85 4.1965
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002538 5484149 Isolate United States North America
Gene Location Start: 3427095;  End: 3428582  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 31 373 2.3e-154 0.9941520467836257

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11318 AmyAc_bac_fung_AmyA 0.0 3 404 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.
PRK09441 PRK09441 0.0 1 490 1 479
cytoplasmic alpha-amylase; Reviewed
cd11314 AmyAc_arch_bac_plant_AmyA 5.94e-55 6 406 2 295
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 2.63e-38 12 490 20 443
Glycosidase [Carbohydrate transport and metabolism].
PLN02784 PLN02784 2.78e-18 6 372 505 819
alpha-amylase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AUC30917.1 0.0 1 495 1 495
AKR88611.1 0.0 1 495 1 495
QKY98858.1 0.0 1 495 1 495
QJM41860.1 0.0 1 495 1 495
ATR52277.1 0.0 1 495 1 495

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1UD2_A 1.67e-145 3 490 4 478
Crystalstructure 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]
1UD3_A 1.67e-145 3 490 4 478
ChainA, amylase [Bacillus sp. KSM-K38]
1OB0_A 2.84e-139 3 490 4 481
Kineticstabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface [Bacillus licheniformis]
1W9X_A 6.06e-138 3 490 2 479
ChainA, Alpha Amylase [Sutcliffiella halmapala]
6TOY_A 6.47e-138 3 490 4 481
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P26613 0.0 1 494 1 494
Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 SV=3
P26612 0.0 1 495 1 495
Cytoplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=amyA PE=1 SV=3
P06278 5.11e-136 3 490 33 510
Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P19571 8.74e-136 3 490 39 516
Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P06279 1.31e-134 3 490 39 515
Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000047 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002538_03296.