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CAZyme Information: MGYG000003433_00559

You are here: Home > Sequence: MGYG000003433_00559

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 CAG-485 sp900766975
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900766975
CAZyme ID MGYG000003433_00559
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
612 66301.05 5.5083
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003433 2173228 MAG Fiji Oceania
Gene Location Start: 8110;  End: 9948  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003433_00559.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 66 340 1.4e-58 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 1.32e-121 37 369 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.
PLN00196 PLN00196 1.10e-56 37 421 26 427
alpha-amylase; Provisional
PLN02784 PLN02784 1.59e-55 37 422 504 894
alpha-amylase
PLN02361 PLN02361 4.82e-51 37 421 13 401
alpha-amylase
PRK09441 PRK09441 8.59e-39 36 360 4 393
cytoplasmic alpha-amylase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADE83209.1 5.22e-121 24 405 16 397
QVJ79591.1 1.03e-119 24 416 16 418
QUB87110.1 2.05e-115 29 392 21 378
AKU69472.1 2.05e-115 29 392 21 378
QUB72338.1 1.61e-114 29 405 21 392

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 9.17e-52 37 421 2 402
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 1.26e-49 37 421 3 403
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 7.17e-46 37 421 3 404
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPS_A 1.12e-45 37 421 3 404
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
1HT6_A 1.12e-45 37 421 3 404
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P04063 8.75e-51 37 421 26 426
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
P17654 1.35e-48 37 421 33 433
Alpha-amylase OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.1 PE=1 SV=2
Q8VZ56 2.80e-48 37 421 27 422
Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1
P27934 5.06e-47 37 421 27 425
Alpha-amylase isozyme 3E OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.4 PE=2 SV=1
P17859 9.48e-47 37 419 25 420
Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 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
0.000584 0.998333 0.000228 0.000334 0.000272 0.000230

TMHMM  Annotations      download full data without filtering help

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