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CAZyme Information: MGYG000001360_02099

You are here: Home > Sequence: MGYG000001360_02099

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 salivae
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella salivae
CAZyme ID MGYG000001360_02099
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
615 MGYG000001360_1|CGC33 69275.8 7.6325
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001360 3139873 Isolate not provided not provided
Gene Location Start: 2501270;  End: 2503117  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001360_02099.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 58 351 4e-50 0.9688581314878892

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 3.40e-122 29 380 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 4.87e-42 29 390 13 363
alpha-amylase
PRK09441 PRK09441 9.32e-41 28 369 4 391
cytoplasmic alpha-amylase; Reviewed
PLN02784 PLN02784 2.60e-40 29 390 504 853
alpha-amylase
PLN00196 PLN00196 1.77e-32 27 396 24 393
alpha-amylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VEH14340.1 0.0 1 615 1 615
ALO47847.1 7.64e-199 1 593 1 569
EFC71671.1 2.48e-194 1 613 1 585
QUB70324.1 1.06e-147 1 556 1 613
QUB72338.1 2.64e-145 1 561 1 618

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 1.62e-32 29 408 2 377
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 1.63e-30 29 396 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]
2QPS_A 6.45e-26 29 410 3 381
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
1HT6_A 8.70e-26 29 408 3 379
CrystalStructure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 [Hordeum vulgare],1P6W_A Crystal structure of barley alpha-amylase isozyme 1 (AMY1) in complex with the substrate analogue, methyl 4I,4II,4III-tri-thiomaltotetraoside (thio-DP4) [Hordeum vulgare],1RPK_A Crystal structure of barley alpha-amylase isozyme 1 (amy1) in complex with acarbose [Hordeum vulgare]
3BSG_A 9.75e-26 29 408 3 379
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 1.16e-34 8 433 8 413
Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1
Q8VZ56 5.64e-33 29 431 27 423
Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1
P04063 1.30e-31 29 408 26 401
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
P27934 1.51e-31 1 433 1 428
Alpha-amylase isozyme 3E OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.4 PE=2 SV=1
Q94A41 3.70e-31 29 390 497 846
Alpha-amylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=AMY3 PE=1 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
0.000219 0.999169 0.000158 0.000149 0.000140 0.000132

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001360_02099.