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CAZyme Information: MGYG000003346_02680

You are here: Home > Sequence: MGYG000003346_02680

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 sp900554545
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900554545
CAZyme ID MGYG000003346_02680
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
676 MGYG000003346_91|CGC1 73930.57 4.2667
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003346 3265104 MAG China Asia
Gene Location Start: 11245;  End: 13275  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003346_02680.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 58 339 1.9e-51 0.9619377162629758

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 7.96e-121 29 363 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 3.75e-48 29 416 13 397
alpha-amylase
PRK09441 PRK09441 2.84e-47 28 396 4 432
cytoplasmic alpha-amylase; Reviewed
PLN00196 PLN00196 9.03e-38 9 418 6 425
alpha-amylase; Provisional
PLN02784 PLN02784 1.37e-35 29 376 504 854
alpha-amylase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB54439.1 5.25e-205 1 674 1 670
QUB49498.1 1.05e-204 1 674 1 670
QUB52626.1 1.49e-204 1 674 1 670
QUB75387.1 6.83e-204 1 674 1 673
ATV30590.1 1.56e-201 1 674 1 670

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 1.10e-35 29 392 2 375
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 2.82e-35 29 381 3 369
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]
3BSG_A 2.89e-34 29 423 3 407
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSH_A 7.22e-34 29 392 3 377
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPS_A 1.14e-33 29 392 3 377
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
Q8VZ56 1.09e-38 29 421 27 423
Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1
Q8LFG1 3.78e-37 29 418 27 411
Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1
P17859 2.06e-36 29 380 25 387
Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1
P04063 9.21e-35 29 392 26 399
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
P17654 2.60e-34 29 381 33 399
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 0.998948 0.000221 0.000166 0.000160 0.000151

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003346_02680.