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CAZyme Information: MGYG000004779_00001

You are here: Home > Sequence: MGYG000004779_00001

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 UMGS1397 sp900551425
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1397; UMGS1397 sp900551425
CAZyme ID MGYG000004779_00001
CAZy Family GH13
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
731 MGYG000004779_1|CGC1 81120.43 4.4336
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004779 2688004 MAG China Asia
Gene Location Start: 364;  End: 2559  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004779_00001.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 338 630 6.3e-30 0.9163879598662207

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11313 AmyAc_arch_bac_AmyA 6.96e-36 322 677 7 321
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 5.29e-22 322 627 2 253
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 1.59e-12 322 664 3 394
Glycosidase [Carbohydrate transport and metabolism].
pfam00128 Alpha-amylase 5.34e-12 340 630 2 325
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.
smart00642 Aamy 3.85e-10 326 411 3 92
Alpha-amylase domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AEE96957.1 5.21e-167 65 730 20 681
QHT61281.1 2.82e-161 59 704 13 654
AZN42601.1 2.25e-155 87 728 44 695
VEH99811.1 5.03e-22 335 692 53 409
ARK12440.1 8.13e-22 299 708 37 447

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4GKL_A 8.08e-21 346 645 29 316
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]
3DHU_A 1.70e-14 328 636 16 319
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]
2ZE0_A 1.20e-12 319 630 8 366
Alpha-glucosidaseGSJ [Geobacillus sp. HTA-462]
5ZCB_A 3.37e-11 323 630 12 366
Crystalstructure of Alpha-glucosidase [Bacillus sp. (in: Bacteria)]
5ZCC_A 3.37e-11 323 630 12 366
Crystalstructure of Alpha-glucosidase in complex with maltose [Bacillus sp. (in: Bacteria)],5ZCD_A Crystal structure of Alpha-glucosidase in complex with maltotriose [Bacillus sp. (in: Bacteria)],5ZCE_A Crystal structure of Alpha-glucosidase in complex with maltotetraose [Bacillus sp. (in: Bacteria)]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P14898 4.29e-10 341 699 165 530
Alpha-amylase 2 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyB PE=1 SV=2
O05242 5.58e-10 322 630 11 366
Probable oligo-1,6-glucosidase 3 OS=Bacillus subtilis (strain 168) OX=224308 GN=yugT PE=3 SV=2
P43473 8.95e-09 322 630 13 373
Alpha-glucosidase OS=Pediococcus pentosaceus OX=1255 GN=agl PE=3 SV=1
A6VP15 1.95e-08 314 475 240 405
1,4-alpha-glucan branching enzyme GlgB OS=Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z) OX=339671 GN=glgB PE=3 SV=1
P80099 2.17e-08 351 630 32 315
4-alpha-glucanotransferase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=mgtA PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000057 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004779_00001.