logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003152_00420

You are here: Home > Sequence: MGYG000003152_00420

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 denticola
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella denticola
CAZyme ID MGYG000003152_00420
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
671 MGYG000003152_2|CGC3 74089.86 8.4784
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003152 2774939 MAG United States North America
Gene Location Start: 125317;  End: 127332  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003152_00420.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 61 344 2.1e-53 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 1.22e-130 32 368 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.
PLN02361 PLN02361 9.55e-49 32 418 13 397
alpha-amylase
PRK09441 PRK09441 1.73e-48 30 359 3 392
cytoplasmic alpha-amylase; Reviewed
PLN02784 PLN02784 1.19e-42 32 397 504 868
alpha-amylase
cd11318 AmyAc_bac_fung_AmyA 3.67e-36 31 360 2 391
Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB90758.1 0.0 1 671 1 671
QUI94094.1 0.0 1 671 1 671
AEA20882.1 0.0 1 671 1 671
QUB88375.1 0.0 1 671 1 671
QUB70315.1 0.0 1 671 1 671

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 3.15e-34 32 418 2 398
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 6.77e-32 32 418 3 400
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPS_A 2.67e-31 32 418 3 400
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSG_A 1.03e-30 32 418 3 400
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3WN6_A 1.19e-30 32 395 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8LFG1 6.33e-39 32 418 27 409
Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1
Q8VZ56 1.11e-36 32 418 27 418
Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1
P08117 2.77e-35 32 399 27 386
Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1
Q94A41 3.50e-34 32 397 497 861
Alpha-amylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=AMY3 PE=1 SV=1
P04063 4.13e-34 11 418 6 422
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3

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
0.001096 0.751619 0.246347 0.000360 0.000294 0.000264

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003152_00420.