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CAZyme Information: MGYG000002905_00429

You are here: Home > Sequence: MGYG000002905_00429

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-279 sp900541935
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-279; CAG-279 sp900541935
CAZyme ID MGYG000002905_00429
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
705 MGYG000002905_6|CGC1 78471.36 5.4635
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002905 2448974 MAG China Asia
Gene Location Start: 14962;  End: 17079  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002905_00429.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 68 344 8.6e-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 9.50e-121 39 373 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 3.69e-59 39 425 13 401
alpha-amylase
PLN00196 PLN00196 1.34e-52 39 426 26 428
alpha-amylase; Provisional
PLN02784 PLN02784 6.53e-52 39 425 504 893
alpha-amylase
PRK09441 PRK09441 1.21e-37 38 364 4 393
cytoplasmic alpha-amylase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCS84551.1 9.03e-141 19 650 12 635
AXV49304.1 8.67e-135 18 627 11 628
QNT66936.1 1.26e-134 18 626 11 624
QUI94094.1 3.42e-134 18 688 11 663
QUB70315.1 4.81e-134 18 627 11 628

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 3.24e-50 39 426 2 403
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 1.06e-47 39 426 3 404
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 1.49e-47 39 425 3 404
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
1HT6_A 1.49e-47 39 425 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]
2QPU_A 2.04e-47 39 425 3 404
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
Q8VZ56 6.52e-53 37 425 25 422
Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1
P04063 3.08e-49 39 426 26 427
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
P17859 3.70e-49 39 423 25 420
Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1
P27932 9.25e-47 39 429 30 432
Alpha-amylase isozyme 3A OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.2 PE=2 SV=2
P08117 9.74e-47 39 425 27 410
Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 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
0.000278 0.998974 0.000199 0.000183 0.000169 0.000156

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002905_00429.