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CAZyme Information: MGYG000003119_00260

You are here: Home > Sequence: MGYG000003119_00260

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 Capnocytophaga ochracea
Lineage Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Flavobacteriaceae; Capnocytophaga; Capnocytophaga ochracea
CAZyme ID MGYG000003119_00260
CAZy Family GH13
CAZyme Description Alpha-amylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
469 MGYG000003119_4|CGC1 53602.19 6.4463
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003119 2451559 MAG United States North America
Gene Location Start: 48549;  End: 49958  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 66 363 4.9e-134 0.9965397923875432

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09441 PRK09441 3.46e-180 40 466 1 479
cytoplasmic alpha-amylase; Reviewed
cd11314 AmyAc_arch_bac_plant_AmyA 1.96e-108 44 387 1 299
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.
cd11318 AmyAc_bac_fung_AmyA 5.47e-76 42 380 1 390
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.
PLN00196 PLN00196 1.99e-40 31 378 13 365
alpha-amylase; Provisional
PLN02784 PLN02784 3.26e-32 40 366 500 824
alpha-amylase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ACU92189.1 0.0 1 469 1 469
QLF50014.1 0.0 1 469 1 469
AVM55753.1 0.0 1 469 1 469
ALC97351.1 0.0 1 469 1 469
ASF41659.1 8.02e-269 1 469 1 469

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1MWO_A 9.58e-110 44 466 11 430
CrystalStructure Analysis of the Hyperthermostable Pyrocoocus woesei alpha-amylase [Pyrococcus woesei],1MXD_A Structure of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei [Pyrococcus woesei],1MXG_A Crystal Structure of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in complex with acarbose [Pyrococcus woesei]
3QGV_A 2.73e-106 44 466 11 430
Crystalstructure of a thermostable amylase variant [Pyrococcus woesei]
4UZU_A 3.76e-44 42 465 5 478
Three-dimensionalstructure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
1HVX_A 1.02e-43 42 465 5 480
BACILLUSSTEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]
6AG0_A 7.22e-42 42 465 32 507
TheX-ray Crystallographic Structure of Maltooligosaccharide-forming Amylase from Bacillus stearothermophilus STB04 [Geobacillus stearothermophilus],6AG0_C The X-ray Crystallographic Structure of Maltooligosaccharide-forming Amylase from Bacillus stearothermophilus STB04 [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P06279 9.29e-43 42 465 39 514
Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P26613 5.12e-41 42 467 3 491
Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 SV=3
P26612 9.92e-41 42 467 3 491
Cytoplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=amyA PE=1 SV=3
P19571 1.24e-38 30 465 23 515
Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
Q8VZ56 1.89e-38 44 412 27 404
Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000055 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003119_00260.