logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003662_01525

You are here: Home > Sequence: MGYG000003662_01525

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 sp900771975
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900771975
CAZyme ID MGYG000003662_01525
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
668 MGYG000003662_68|CGC1 74777.08 5.1114
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003662 2760601 MAG Peru South America
Gene Location Start: 37694;  End: 39700  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003662_01525.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 58 341 1.6e-46 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 2.37e-115 29 365 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 6.74e-49 29 366 13 352
alpha-amylase
PLN02784 PLN02784 8.13e-43 29 366 504 842
alpha-amylase
PRK09441 PRK09441 1.40e-36 27 357 3 392
cytoplasmic alpha-amylase; Reviewed
PLN00196 PLN00196 6.59e-30 11 365 6 375
alpha-amylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB75387.1 1.63e-251 1 668 1 675
AKU69270.1 2.31e-248 1 668 1 674
QKH89892.1 2.00e-245 18 668 1 658
QUB87660.1 2.74e-245 18 668 1 657
QUB80123.1 7.28e-245 1 668 1 675

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 2.63e-28 29 365 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]
3WN6_A 3.18e-26 29 365 3 351
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 1.19e-25 29 365 3 352
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPS_A 1.92e-25 29 365 3 352
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPU_A 1.92e-25 29 365 3 352
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8LFG1 6.10e-42 29 366 27 364
Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1
Q94A41 8.07e-34 29 356 497 825
Alpha-amylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=AMY3 PE=1 SV=1
P17859 1.44e-32 5 366 4 371
Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1
P04063 5.56e-29 2 365 4 374
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
P27933 2.81e-28 10 386 6 400
Alpha-amylase isozyme 3D OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.3 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
0.000421 0.998786 0.000219 0.000213 0.000181 0.000170

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003662_01525.