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CAZyme Information: MGYG000003825_00629

You are here: Home > Sequence: MGYG000003825_00629

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 UBA1777 sp900549645
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA1777; UBA1777 sp900549645
CAZyme ID MGYG000003825_00629
CAZy Family GH13
CAZyme Description Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
426 MGYG000003825_10|CGC1 48633.9 4.8146
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003825 2022533 MAG United States North America
Gene Location Start: 40244;  End: 41524  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003825_00629.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 25 314 9.3e-50 0.9230769230769231

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11313 AmyAc_arch_bac_AmyA 3.30e-172 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.
cd00551 AmyAc_family 1.39e-34 13 309 1 253
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.
COG0366 AmyA 1.49e-34 12 312 1 355
Glycosidase [Carbohydrate transport and metabolism].
cd11347 AmyAc_1 2.00e-34 32 311 28 344
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.
cd11349 AmyAc_3 9.26e-34 13 313 2 390
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SDR97044.1 2.36e-192 1 424 1 436
ADK68587.1 4.69e-192 1 426 1 425
AKT47795.1 2.13e-191 1 424 1 428
ADZ83055.1 3.48e-169 1 424 1 425
AHV98322.1 8.63e-169 1 426 1 427

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3DHU_A 3.42e-132 5 425 6 426
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 1.50e-80 9 313 3 292
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 7.59e-23 15 204 215 427
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 7.81e-23 15 204 215 427
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 7.93e-23 15 204 235 447
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 1.46e-25 13 313 249 538
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
Q9KY04 2.33e-22 15 204 206 418
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 2 OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=glgE2 PE=1 SV=1
Q9L1K2 4.23e-22 15 204 215 427
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=glgE1 PE=1 SV=1
Q1D651 5.59e-22 15 204 206 419
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Myxococcus xanthus (strain DK1622) OX=246197 GN=glgE PE=3 SV=1
Q8KAR6 1.81e-21 15 204 213 426
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

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 MGYG000003825_00629.