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CAZyme Information: MGYG000003461_01175

You are here: Home > Sequence: MGYG000003461_01175

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 sp900553595
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900553595
CAZyme ID MGYG000003461_01175
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
674 MGYG000003461_354|CGC1 75077.73 7.7042
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003461 2310521 MAG Fiji Oceania
Gene Location Start: 2214;  End: 4238  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003461_01175.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 58 345 3.7e-44 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 1.39e-110 29 369 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 1.03e-38 29 356 13 335
alpha-amylase
PRK09441 PRK09441 6.57e-35 28 343 4 366
cytoplasmic alpha-amylase; Reviewed
PLN02784 PLN02784 7.81e-33 29 419 504 889
alpha-amylase
PLN00196 PLN00196 3.25e-30 29 418 26 422
alpha-amylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB52626.1 3.59e-223 1 674 1 672
QUB49498.1 5.83e-222 1 674 1 672
QUB54439.1 8.25e-222 1 674 1 672
BAU18256.1 7.04e-218 1 674 1 672
ATV26526.1 4.01e-217 1 674 1 672

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 1.43e-31 29 418 2 397
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 1.64e-30 29 418 3 398
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 1.02e-29 29 418 3 399
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSH_A 1.57e-29 29 418 3 399
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
1HT6_A 6.18e-29 29 418 3 399
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
P08117 1.46e-37 29 418 27 405
Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1
Q8VZ56 8.36e-33 29 371 27 373
Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1
Q8LFG1 3.70e-31 25 356 23 347
Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1
P04747 1.06e-30 29 362 26 368
Alpha-amylase type B isozyme (Fragment) OS=Hordeum vulgare OX=4513 GN=AMY1.3 PE=2 SV=1
P04063 1.14e-30 29 418 26 421
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
0.000370 0.998858 0.000168 0.000217 0.000190 0.000178

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003461_01175.