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CAZyme Information: MGYG000004329_01007

You are here: Home > Sequence: MGYG000004329_01007

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 Prevotellamassilia sp900539625
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia sp900539625
CAZyme ID MGYG000004329_01007
CAZy Family GH13
CAZyme Description Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
552 MGYG000004329_16|CGC1 62879.04 6.3837
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004329 2571737 MAG Israel Asia
Gene Location Start: 22972;  End: 24630  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004329_01007.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 26 393 8.4e-182 0.9973333333333333

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11349 AmyAc_3 0.0 2 449 3 456
Alpha amylase catalytic domain found in an uncharacterized protein family. 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.
cd11313 AmyAc_arch_bac_AmyA 9.46e-46 1 452 6 336
Alpha amylase catalytic domain found in archaeal and bacterial 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 firmicutes, bacteroidetes, and proteobacteria. 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.
cd11347 AmyAc_1 1.51e-41 1 390 2 349
Alpha amylase catalytic domain found in an uncharacterized protein family. 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.
COG0366 AmyA 4.83e-25 2 498 3 490
Glycosidase [Carbohydrate transport and metabolism].
cd00551 AmyAc_family 2.33e-21 2 389 2 259
Alpha amylase catalytic domain family. 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; and 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 this 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QFQ12053.1 4.82e-258 2 551 6 551
QRO26211.1 2.87e-248 1 551 8 562
ADY36223.1 6.68e-247 1 551 8 562
QVJ81385.1 4.69e-239 1 551 8 549
ADE81408.1 3.83e-238 1 551 8 549

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4GKL_A 9.09e-16 1 353 7 262
Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana]
3DHU_A 1.03e-14 38 354 35 284
Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
4E2O_A 9.07e-11 29 538 42 444
Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
7JJT_A 2.29e-09 76 552 82 522
ChainA, Alpha-amylase [Ruminococcus bromii]
6LGG_A 7.64e-09 1 255 44 239
Bombyxmori GH13 sucrose hydrolase mutant E322Q complexed with sucrose [Bombyx mori],6LGG_B Bombyx mori GH13 sucrose hydrolase mutant E322Q complexed with sucrose [Bombyx mori],6LGH_A Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate [Bombyx mori],6LGH_B Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate [Bombyx mori],6LGI_A Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate complexed with fructose [Bombyx mori],6LGI_B Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate complexed with fructose [Bombyx mori]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P07190 2.06e-10 3 255 29 221
Maltase A1 OS=Drosophila melanogaster OX=7227 GN=Mal-A1 PE=2 SV=2
O16098 8.18e-09 1 255 87 280
Maltase 1 OS=Drosophila virilis OX=7244 GN=Mal-B1 PE=3 SV=2
P31797 3.18e-07 1 386 44 391
Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
Q8KAR6 4.08e-07 232 340 370 486
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) OX=194439 GN=glgE PE=3 SV=1
Q64319 9.43e-07 85 314 172 359
Neutral and basic amino acid transport protein rBAT OS=Rattus norvegicus OX=10116 GN=Slc3a1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.997722 0.002277 0.000039 0.000004 0.000002 0.000006

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004329_01007.