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CAZyme Information: MGYG000004632_01893

You are here: Home > Sequence: MGYG000004632_01893

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 sp002300055
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp002300055
CAZyme ID MGYG000004632_01893
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
680 MGYG000004632_35|CGC1 74825.53 8.8877
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004632 2937832 MAG Germany Europe
Gene Location Start: 24321;  End: 26363  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004632_01893.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 59 340 8.7e-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 6.04e-115 30 368 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 1.38e-48 26 417 9 396
alpha-amylase
PRK09441 PRK09441 3.98e-42 26 397 1 441
cytoplasmic alpha-amylase; Reviewed
PLN02784 PLN02784 2.53e-35 30 418 504 889
alpha-amylase
PLN00196 PLN00196 8.80e-35 30 370 26 378
alpha-amylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB52626.1 4.96e-217 3 609 2 617
QUB49498.1 4.96e-217 3 609 2 617
QUB54439.1 5.67e-216 3 609 2 617
ATV28867.1 8.03e-216 3 609 2 617
ATV37914.1 1.61e-215 3 609 2 617

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 2.03e-37 30 367 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 2.11e-33 30 367 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 4.60e-33 27 417 1 399
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPS_A 5.36e-33 27 417 1 399
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPU_A 1.81e-32 27 370 1 355
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 6.03e-38 30 417 27 408
Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1
P04063 1.27e-36 2 367 3 374
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
P08117 1.83e-36 30 364 27 354
Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1
P17859 2.88e-36 30 380 25 383
Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1
P04747 7.97e-35 2 358 3 365
Alpha-amylase type B isozyme (Fragment) OS=Hordeum vulgare OX=4513 GN=AMY1.3 PE=2 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
0.000318 0.998882 0.000197 0.000201 0.000185 0.000175

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004632_01893.