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CAZyme Information: MGYG000001839_00359

You are here: Home > Sequence: MGYG000001839_00359

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173;
CAZyme ID MGYG000001839_00359
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
606 66119.67 5.3575
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001839 2457764 MAG Denmark Europe
Gene Location Start: 28921;  End: 30741  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001839_00359.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 61 338 1.1e-55 0.972318339100346

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 2.17e-120 33 367 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 33 419 13 401
alpha-amylase
PLN00196 PLN00196 6.18e-57 33 419 26 427
alpha-amylase; Provisional
PLN02784 PLN02784 8.34e-54 33 420 504 894
alpha-amylase
PRK09441 PRK09441 6.72e-43 32 357 4 392
cytoplasmic alpha-amylase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADE83209.1 1.16e-127 20 414 16 410
VEH14340.1 6.37e-126 12 402 8 416
ALO47847.1 6.04e-122 21 402 18 400
QVJ79591.1 1.96e-121 20 414 16 418
QUB87110.1 9.76e-119 25 403 21 392

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 2.25e-54 33 419 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 6.18e-53 33 419 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]
3BSH_A 7.65e-51 33 419 3 404
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSG_A 2.82e-50 33 419 3 404
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPS_A 4.41e-50 33 419 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
P08117 2.17e-55 33 420 27 411
Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1
P04063 2.18e-53 33 419 26 426
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
Q8VZ56 1.03e-52 33 419 27 422
Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1
P27939 3.78e-52 33 423 28 430
Alpha-amylase isozyme 3C OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.7 PE=2 SV=2
P27932 4.05e-52 33 423 30 432
Alpha-amylase isozyme 3A OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.2 PE=2 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
0.000341 0.998771 0.000206 0.000243 0.000221 0.000196

TMHMM  Annotations      download full data without filtering help

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