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CAZyme Information: MGYG000000899_01336

You are here: Home > Sequence: MGYG000000899_01336

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 UMGS1241 sp900549955
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-138; UMGS1241; UMGS1241 sp900549955
CAZyme ID MGYG000000899_01336
CAZy Family GH13
CAZyme Description Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
426 MGYG000000899_26|CGC1 47906.37 5.6485
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000899 1597492 MAG Denmark Europe
Gene Location Start: 15419;  End: 16699  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000899_01336.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 25 316 9.2e-46 0.9297658862876255

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11313 AmyAc_arch_bac_AmyA 4.02e-176 9 348 2 329
Alpha amylase catalytic domain found in archaeal and 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 firmicutes, bacteroidetes, and proteobacteria. 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.
cd11347 AmyAc_1 3.51e-38 37 358 35 391
Alpha amylase catalytic domain found in an uncharacterized protein family. 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.
cd11344 AmyAc_GlgE_like 9.73e-38 26 200 20 214
Alpha amylase catalytic domain found in GlgE-like proteins. GlgE is a (1,4)-a-D-glucan:phosphate a-D-maltosyltransferase, involved in a-glucan biosynthesis in bacteria. It is also an anti-tuberculosis drug target. GlgE isoform I from Streptomyces coelicolor has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. GlgE from Streptomyces coelicolor forms a homodimer with each subunit comprising five domains (A, B, C, N, and S) and 2 inserts. Domain A is a catalytic alpha-amylase-type domain that along with domain N, which has a beta-sandwich fold and forms the core of the dimer interface, binds cyclodextrins. Domain A, B, and the 2 inserts define a well conserved donor pocket that binds maltose. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, indicating that the hydrophobic patch overlaps with the acceptor binding site. This is not the case in M. tuberculosis GlgE because cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. Domain C is hypothesized to help stabilize domain A and could be involved in substrate binding. Domain S is a helix bundle that is inserted within the N domain and it plays a role in the dimer interface and interacts directly with domain B. 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 4.72e-32 13 316 2 359
Glycosidase [Carbohydrate transport and metabolism].
cd11338 AmyAc_CMD 6.47e-32 26 313 53 342
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBH26772.1 3.44e-180 1 424 1 436
BBH26770.1 3.44e-180 1 424 1 436
BBH26774.1 3.44e-180 1 424 1 436
AHV98329.1 2.09e-174 1 424 1 425
QSF43712.1 6.89e-173 1 424 1 425

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3DHU_A 4.84e-150 4 426 5 427
Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
4GKL_A 2.25e-86 9 332 3 311
Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana]
5VSJ_A 6.90e-25 22 319 226 521
ScoGlgEI-V279S in complex with a pyrolidene-based ethyl-phosphonate compound [Streptomyces coelicolor A3(2)],5VSJ_B Sco GlgEI-V279S in complex with a pyrolidene-based ethyl-phosphonate compound [Streptomyces coelicolor A3(2)],5VT4_A Sco GlgEI-V279S in complex with a pyrolidene-based methyl-phosphonate compound [Streptomyces coelicolor A3(2)],5VT4_B Sco GlgEI-V279S in complex with a pyrolidene-based methyl-phosphonate compound [Streptomyces coelicolor A3(2)],5VT4_C Sco GlgEI-V279S in complex with a pyrolidene-based methyl-phosphonate compound [Streptomyces coelicolor A3(2)],5VT4_D Sco GlgEI-V279S in complex with a pyrolidene-based methyl-phosphonate compound [Streptomyces coelicolor A3(2)]
4U2Y_A 7.12e-25 22 319 226 521
ScoGlgEI-V279S in Complex with Reaction Intermediate Azasugar [Streptomyces coelicolor A3(2)],4U2Y_B Sco GlgEI-V279S in Complex with Reaction Intermediate Azasugar [Streptomyces coelicolor A3(2)],4U2Z_A X-ray crystal structure of an Sco GlgEI-V279S/1,2,2-trifluromaltose complex [Streptomyces coelicolor A3(2)],4U2Z_B X-ray crystal structure of an Sco GlgEI-V279S/1,2,2-trifluromaltose complex [Streptomyces coelicolor A3(2)],4U31_A Sco GlgEI-V279S in Complex with maltose-C-phosphonate [Streptomyces coelicolor A3(2)],4U31_B Sco GlgEI-V279S in Complex with maltose-C-phosphonate [Streptomyces coelicolor A3(2)],7MEL_A Chain A, Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 [Streptomyces coelicolor A3(2)],7MEL_B Chain B, Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 [Streptomyces coelicolor A3(2)],7MGY_A Chain A, Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 [Streptomyces coelicolor A3(2)],7MGY_B Chain B, Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 [Streptomyces coelicolor A3(2)]
3ZSS_A 4.23e-24 22 319 246 541
Apoform of GlgE isoform 1 from Streptomyces coelicolor [Streptomyces coelicolor],3ZSS_B Apo form of GlgE isoform 1 from Streptomyces coelicolor [Streptomyces coelicolor],3ZSS_C Apo form of GlgE isoform 1 from Streptomyces coelicolor [Streptomyces coelicolor],3ZSS_D Apo form of GlgE isoform 1 from Streptomyces coelicolor [Streptomyces coelicolor],3ZST_A GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin bound [Streptomyces coelicolor],3ZST_B GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin bound [Streptomyces coelicolor],3ZT5_A GlgE isoform 1 from Streptomyces coelicolor with maltose bound [Streptomyces coelicolor],3ZT5_B GlgE isoform 1 from Streptomyces coelicolor with maltose bound [Streptomyces coelicolor],3ZT5_C GlgE isoform 1 from Streptomyces coelicolor with maltose bound [Streptomyces coelicolor],3ZT5_D GlgE isoform 1 from Streptomyces coelicolor with maltose bound [Streptomyces coelicolor],3ZT6_A GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT6_B GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT6_C GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT6_D GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT7_A GlgE isoform 1 from Streptomyces coelicolor with beta-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT7_B GlgE isoform 1 from Streptomyces coelicolor with beta-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT7_C GlgE isoform 1 from Streptomyces coelicolor with beta-cyclodextrin and maltose bound [Streptomyces coelicolor],3ZT7_D GlgE isoform 1 from Streptomyces coelicolor with beta-cyclodextrin and maltose bound [Streptomyces coelicolor]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
L8B068 4.46e-32 14 372 250 600
Alpha-amylase MalA OS=Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1) OX=1227453 GN=malA PE=1 SV=1
Q3J3M8 1.71e-27 15 290 215 494
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) OX=272943 GN=glgE PE=3 SV=3
Q9I1W4 2.28e-27 10 350 207 559
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=glgE PE=3 SV=1
Q9JN46 2.45e-27 26 290 212 476
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2
Q2RTZ1 7.90e-27 26 289 255 518
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1) OX=269796 GN=glgE 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
1.000056 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000899_01336.