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CAZyme Information: MGYG000002653_00847

You are here: Home > Sequence: MGYG000002653_00847

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 Prevotella sp002251295
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp002251295
CAZyme ID MGYG000002653_00847
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
684 MGYG000002653_11|CGC1 76129.48 7.6737
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002653 3045320 MAG United Republic of Tanzania Africa
Gene Location Start: 38687;  End: 40741  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002653_00847.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 68 354 4.9e-45 0.9653979238754326

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 4.93e-113 39 377 1 300
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 1.81e-42 39 365 13 335
alpha-amylase
PRK09441 PRK09441 6.34e-38 38 352 4 366
cytoplasmic alpha-amylase; Reviewed
PLN00196 PLN00196 7.52e-30 37 391 24 389
alpha-amylase; Provisional
PLN02784 PLN02784 1.28e-29 39 373 504 837
alpha-amylase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB52626.1 5.00e-236 12 684 2 672
QUB49498.1 1.15e-234 12 684 2 672
QUB54439.1 1.15e-234 12 684 2 672
ATV30590.1 1.73e-231 12 684 2 672
APW31650.1 2.46e-231 12 684 2 672

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3WN6_A 9.34e-31 39 373 3 347
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]
1AMY_A 5.62e-30 39 377 2 350
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]
3BSH_A 8.67e-27 39 435 3 407
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPS_A 2.52e-26 39 427 3 399
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
6IWK_A 9.80e-26 37 423 16 407
TheStructure of Maltooligosaccharide-forming Amylase from Pseudomonas saccharophila STB07 [Pelomonas saccharophila]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8VZ56 2.65e-35 21 392 8 385
Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1
P08117 8.52e-32 39 356 27 334
Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1
P17859 9.70e-32 39 389 25 382
Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1
P17654 8.05e-30 39 373 33 377
Alpha-amylase OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.1 PE=1 SV=2
Q8LFG1 1.08e-29 39 365 27 347
Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1

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
0.000700 0.998373 0.000287 0.000219 0.000214 0.000191

TMHMM  Annotations      download full data without filtering help

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