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CAZyme Information: MGYG000001036_00320

You are here: Home > Sequence: MGYG000001036_00320

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-1031 sp900752535
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-1031; CAG-1031 sp900752535
CAZyme ID MGYG000001036_00320
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
818 MGYG000001036_55|CGC1 90358.19 4.8296
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001036 3018511 MAG Sweden Europe
Gene Location Start: 19820;  End: 22276  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001036_00320.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 61 337 1.5e-59 0.9688581314878892

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11314 AmyAc_arch_bac_plant_AmyA 2.81e-124 32 366 1 302
Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 AmyA from bacteria, archaea, water fleas, and plants. 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.
PLN02361 PLN02361 1.86e-61 32 418 13 401
alpha-amylase
PLN02784 PLN02784 2.26e-58 32 419 504 894
alpha-amylase
PLN00196 PLN00196 7.90e-53 32 418 26 427
alpha-amylase; Provisional
PRK09441 PRK09441 1.87e-43 31 356 4 392
cytoplasmic alpha-amylase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADE83209.1 2.40e-130 5 392 7 390
ALO47847.1 1.03e-129 10 432 9 430
QUB72338.1 1.36e-128 24 438 21 420
QUB87110.1 1.42e-127 24 493 21 470
AKU69472.1 1.42e-127 24 493 21 470

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 4.80e-53 32 418 2 402
CrystalAnd Molecular Structure Of Barley Alpha-Amylase [Hordeum vulgare],1AVA_A Amy2BASI PROTEIN-Protein Complex From Barley Seed [Hordeum vulgare],1AVA_B Amy2BASI PROTEIN-Protein Complex From Barley Seed [Hordeum vulgare],1BG9_A Barley Alpha-Amylase With Substrate Analogue Acarbose [Hordeum vulgare]
3WN6_A 1.46e-50 32 418 3 403
Crystalstructure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group],3WN6_B Crystal structure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group],3WN6_C Crystal structure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group],3WN6_D Crystal structure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group]
2QPU_A 3.14e-48 32 418 3 404
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare],2QPU_B Chain B, Alpha-amylase type A isozyme [Hordeum vulgare],2QPU_C Chain C, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSG_A 2.51e-47 32 418 3 404
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPS_A 3.83e-47 32 418 3 404
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P27934 8.80e-53 32 418 27 425
Alpha-amylase isozyme 3E OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.4 PE=2 SV=1
P08117 2.44e-52 32 419 27 411
Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1
P04063 4.66e-52 32 418 26 426
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
P17859 1.31e-50 32 416 25 420
Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1
P17654 1.60e-49 32 418 33 433
Alpha-amylase OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000332 0.998902 0.000196 0.000201 0.000187 0.000175

TMHMM  Annotations      download full data without filtering help

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