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CAZyme Information: MGYG000001339_00380

You are here: Home > Sequence: MGYG000001339_00380

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 Acetomicrobium hydrogeniformans
Lineage Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae; Acetomicrobium; Acetomicrobium hydrogeniformans
CAZyme ID MGYG000001339_00380
CAZy Family GH13
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1091 MGYG000001339_1|CGC3 127354.51 6.6219
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001339 2123925 Isolate not provided North America
Gene Location Start: 380537;  End: 383812  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 5.4.99.16

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 36 389 4.2e-176 0.9971671388101983

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11334 AmyAc_TreS 0.0 13 459 1 447
Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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.
TIGR02456 treS_nterm 0.0 12 549 1 538
trehalose synthase. Trehalose synthase interconverts maltose and alpha, alpha-trehalose by transglucosylation. This is one of at least three mechanisms for biosynthesis of trehalose, an important and widespread compatible solute. However, it is not driven by phosphate activation of sugars and its physiological role may tend toward trehalose degradation. This view is accentuated by numerous examples of fusion to a probable maltokinase domain. The sequence region described by this model is found both as the whole of a trehalose synthase and as the N-terminal region of a larger fusion protein that includes trehalose synthase activity. Several of these fused trehalose synthases have a domain homologous to proteins with maltokinase activity from Actinoplanes missouriensis and Streptomyces coelicolor (). [Energy metabolism, Biosynthesis and degradation of polysaccharides]
cd11333 AmyAc_SI_OligoGlu_DGase 4.06e-130 15 460 1 427
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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.
cd11316 AmyAc_bac2_AmyA 2.03e-118 17 468 1 403
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.
COG0366 AmyA 5.48e-113 17 520 1 505
Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CAJ73822.1 0.0 11 1090 12 1107
QII10851.1 0.0 11 1090 12 1107
QJT10643.1 0.0 8 1089 9 1099
AJF05824.1 0.0 8 1090 10 1108
ACV67337.1 0.0 2 1089 5 1101

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5X7U_A 3.25e-269 8 549 2 541
Trehalosesynthase from Thermobaculum terrenum [Thermobaculum terrenum ATCC BAA-798]
5H2T_A 2.31e-240 10 549 19 560
Structureof trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_B Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_C Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_D Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_E Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_F Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_G Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_H Structure of trehalose synthase [Thermomonospora curvata DSM 43183]
3ZO9_A 1.17e-229 2 549 27 582
ChainA, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],3ZO9_B Chain B, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],3ZOA_A Chain A, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],3ZOA_B Chain B, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],5JY7_A Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_B Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_C Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_D Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_E Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_F Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_G Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_H Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155]
4LXF_A 9.74e-222 3 549 52 603
Crystalstructure of M. tuberculosis TreS [Mycobacterium tuberculosis H37Rv],4LXF_B Crystal structure of M. tuberculosis TreS [Mycobacterium tuberculosis H37Rv]
4TVU_A 3.15e-211 7 561 4 565
Crystalstructure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization [Deinococcus radiodurans R1],4TVU_B Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization [Deinococcus radiodurans R1],4TVU_C Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization [Deinococcus radiodurans R1],4TVU_D Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization [Deinococcus radiodurans R1],4TVU_E Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization [Deinococcus radiodurans R1],4TVU_F Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization [Deinococcus radiodurans R1],4TVU_G Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization [Deinococcus radiodurans R1],4TVU_H Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization [Deinococcus radiodurans R1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0R6E0 6.41e-229 2 549 27 582
Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS PE=1 SV=1
P72235 9.14e-223 11 549 13 562
Trehalose synthase OS=Pimelobacter sp. (strain R48) OX=51662 GN=treS PE=3 SV=1
P9WQ18 2.75e-221 3 549 33 584
Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treS PE=3 SV=1
P9WQ19 2.75e-221 3 549 33 584
Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treS PE=1 SV=1
O06458 4.34e-215 10 562 2 550
Trehalose synthase OS=Thermus thermophilus OX=274 GN=treS PE=3 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
0.999996 0.000028 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001339_00380.