logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004474_01143

You are here: Home > Sequence: MGYG000004474_01143

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 Sodaliphilus sp004557565
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Sodaliphilus; Sodaliphilus sp004557565
CAZyme ID MGYG000004474_01143
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
680 MGYG000004474_24|CGC1 74990.88 5.007
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004474 2861939 MAG Israel Asia
Gene Location Start: 280;  End: 2322  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004474_01143.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 56 346 5.7e-47 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 6.06e-118 29 370 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 2.14e-46 29 418 13 396
alpha-amylase
PRK09441 PRK09441 1.68e-37 27 361 3 392
cytoplasmic alpha-amylase; Reviewed
PLN02784 PLN02784 1.89e-37 29 419 504 889
alpha-amylase
PLN00196 PLN00196 9.87e-35 9 397 6 400
alpha-amylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCS84551.1 6.53e-267 1 619 1 613
QUB70315.1 1.73e-222 11 614 11 624
QNT66936.1 2.54e-222 1 614 1 621
QUI94094.1 3.47e-222 11 614 11 624
QUB92572.1 9.87e-222 11 614 11 624

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 1.13e-35 29 397 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]
3WN6_A 5.27e-33 29 387 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]
3BSG_A 1.77e-28 29 418 3 399
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPS_A 5.15e-28 29 397 3 377
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPU_A 5.15e-28 29 397 3 377
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
P04063 8.09e-36 9 397 6 399
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
P08117 1.17e-35 15 387 13 375
Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1
P17859 3.95e-34 29 397 25 395
Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1
Q8LFG1 4.67e-34 29 418 27 408
Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1
P17654 1.66e-33 9 387 13 399
Alpha-amylase OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.1 PE=1 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
0.000245 0.999092 0.000151 0.000176 0.000162 0.000151

TMHMM  Annotations      download full data without filtering help

start end
7 29