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CAZyme Information: MGYG000000347_01481

You are here: Home > Sequence: MGYG000000347_01481

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 Tener-01 sp001940985
Lineage Bacteria; Firmicutes; Bacilli; ML615J-28; CAG-698; Tener-01; Tener-01 sp001940985
CAZyme ID MGYG000000347_01481
CAZy Family GH13
CAZyme Description Maltodextrin glucosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
628 73533.76 6.7706
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000347 1763421 MAG Sweden Europe
Gene Location Start: 2403;  End: 4289  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.41 2.4.1.25 3.2.1.33 3.2.1.54 3.2.1.135

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 182 504 1.3e-111 0.9902597402597403

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10785 PRK10785 5.33e-164 24 591 17 572
maltodextrin glucosidase; Provisional
cd11338 AmyAc_CMD 6.69e-145 126 549 1 389
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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 1.87e-54 127 588 1 495
Glycosidase [Carbohydrate transport and metabolism].
pfam00128 Alpha-amylase 1.79e-51 182 499 1 325
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.
cd11316 AmyAc_bac2_AmyA 5.40e-47 128 525 2 355
Alpha amylase catalytic domain found in bacterial 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CDM67587.1 7.50e-294 1 626 1 628
AGI39013.1 9.72e-230 4 594 8 598
AGC67978.1 9.72e-230 4 594 8 598
ANW98380.1 9.72e-230 4 594 8 598
ANX00916.1 9.72e-230 4 594 8 598

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5Z0T_A 4.58e-88 111 586 117 595
Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE) [Thermoactinomyces vulgaris],5Z0T_B Thermoactinomyces vulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE) [Thermoactinomyces vulgaris]
1IZJ_A 1.26e-87 111 586 117 595
ChainA, amylase [Thermoactinomyces vulgaris]
1JI1_A 1.76e-87 111 586 117 595
CrystalStructure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 [Thermoactinomyces vulgaris],1JI1_B Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 [Thermoactinomyces vulgaris],1UH3_A Thermoactinomyces vulgaris R-47 alpha-amylase/acarbose complex [Thermoactinomyces vulgaris]
2D0F_A 9.43e-87 111 586 117 595
ChainA, alpha-amylase I [Thermoactinomyces vulgaris]
5BN7_A 2.19e-86 120 575 118 560
Crystalstructure of maltodextrin glucosidase from E.coli at 3.7 A resolution [Escherichia coli K-12]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q60053 1.89e-86 111 586 146 624
Neopullulanase 1 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaI PE=1 SV=1
P21517 8.96e-86 120 575 116 558
Maltodextrin glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=malZ PE=1 SV=5
P29964 1.11e-70 120 626 125 573
Cyclomaltodextrinase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=Teth39_0676 PE=1 SV=2
Q59226 1.15e-67 106 577 107 535
Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
A0A7U9P668 2.20e-67 118 592 126 553
Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1

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
1.000072 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000347_01481.