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CAZyme Information: MGYG000000272_03326

You are here: Home > Sequence: MGYG000000272_03326

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 hominis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella hominis
CAZyme ID MGYG000000272_03326
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
653 73369.05 5.0992
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000272 3991064 Isolate China Asia
Gene Location Start: 2358;  End: 4319  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000272_03326.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 91 383 5.5e-49 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 2.51e-122 62 404 1 301
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.
PRK09441 PRK09441 1.66e-49 61 396 4 393
cytoplasmic alpha-amylase; Reviewed
PLN02361 PLN02361 9.69e-47 62 453 13 397
alpha-amylase
PLN00196 PLN00196 6.53e-43 62 435 26 404
alpha-amylase; Provisional
PLN02784 PLN02784 2.93e-40 62 453 504 889
alpha-amylase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNT66936.1 8.11e-308 1 649 1 622
BCS84551.1 2.17e-238 52 649 19 609
QUB90758.1 1.01e-224 53 649 23 625
QUI94094.1 2.88e-224 53 649 23 625
QUB70315.1 2.88e-224 53 649 23 625

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3WN6_A 2.60e-38 62 431 3 376
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 3.49e-38 62 431 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]
2QPS_A 5.99e-37 62 458 3 405
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSG_A 9.64e-37 62 460 3 407
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSH_A 2.44e-36 62 460 3 407
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
P17654 2.48e-37 62 431 33 406
Alpha-amylase OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.1 PE=1 SV=2
P04063 2.99e-37 62 431 26 399
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
Q8LFG1 1.50e-36 62 453 27 409
Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1
P17859 1.73e-36 62 435 25 399
Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1
P27932 2.10e-35 56 432 24 408
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 LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000058 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000272_03326.