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CAZyme Information: MGYG000002578_00035

You are here: Home > Sequence: MGYG000002578_00035

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 CAG-977 sp900553035
Lineage Bacteria; Proteobacteria; Alphaproteobacteria; RF32; CAG-977; CAG-977; CAG-977 sp900553035
CAZyme ID MGYG000002578_00035
CAZy Family GH13
CAZyme Description Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
706 82254.89 4.9081
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002578 2398245 MAG China Asia
Gene Location Start: 36695;  End: 38815  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.99.16

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 274 494 8.1e-90 0.9809523809523809

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11344 AmyAc_GlgE_like 0.0 248 601 1 355
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.
pfam11896 DUF3416 7.50e-53 47 243 3 185
Domain of unknown function (DUF3416). This presumed domain is functionally uncharacterized. This domain is found in bacteria and archaea. This domain is about 190 amino acids in length. This domain is found associated with pfam00128.
cd11313 AmyAc_arch_bac_AmyA 5.23e-46 252 467 8 201
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.
COG0366 AmyA 5.28e-19 266 521 25 301
Glycosidase [Carbohydrate transport and metabolism].
cd00551 AmyAc_family 7.33e-17 267 523 22 210
Alpha amylase catalytic domain 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; and 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 this 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
QNT69253.1 3.31e-271 44 706 32 682
AEO48121.1 1.40e-260 44 700 32 688
ABC22404.1 1.40e-260 44 700 32 688
QXG82040.1 1.40e-260 44 700 32 688
VBB69867.1 3.22e-257 38 700 20 669

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5VSJ_A 3.75e-179 47 698 21 661
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 7.13e-179 47 698 21 661
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 8.32e-178 47 698 41 681
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]
5CVS_A 3.51e-177 47 698 21 661
GlgEisoform 1 from Streptomyces coelicolor E423A mutant soaked in maltoheptaose [Streptomyces coelicolor],5CVS_B GlgE isoform 1 from Streptomyces coelicolor E423A mutant soaked in maltoheptaose [Streptomyces coelicolor]
4CN4_A 6.63e-177 47 698 41 681
GlgEisoform 1 from Streptomyces coelicolor E423A mutant with 2-deoxy- 2-fluoro-beta-maltosyl modification [Streptomyces coelicolor],4CN4_B GlgE isoform 1 from Streptomyces coelicolor E423A mutant with 2-deoxy- 2-fluoro-beta-maltosyl modification [Streptomyces coelicolor],4CN6_A GlgE isoform 1 from Streptomyces coelicolor E423A mutant with maltose bound [Streptomyces coelicolor],4CN6_B GlgE isoform 1 from Streptomyces coelicolor E423A mutant with maltose bound [Streptomyces coelicolor],5LGV_A GlgE isoform 1 from Streptomyces coelicolor E423A mutant soaked in maltooctaose [Streptomyces coelicolor A3(2)],5LGV_B GlgE isoform 1 from Streptomyces coelicolor E423A mutant soaked in maltooctaose [Streptomyces coelicolor A3(2)]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q2RTZ1 2.79e-261 44 700 32 688
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
Q1D651 4.10e-214 47 688 8 642
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Myxococcus xanthus (strain DK1622) OX=246197 GN=glgE PE=3 SV=1
Q8KAR6 1.11e-212 47 699 23 667
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) OX=194439 GN=glgE PE=3 SV=1
Q3J3M8 2.37e-211 43 698 22 661
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
Q9JN46 4.45e-203 43 645 4 590
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2

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
1.000057 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002578_00035.