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CAZyme Information: MGYG000003633_01084

You are here: Home > Sequence: MGYG000003633_01084

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae; RF16;
CAZyme ID MGYG000003633_01084
CAZy Family GH13
CAZyme Description Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
454 52559.99 5.2568
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003633 1440722 MAG Fiji Oceania
Gene Location Start: 105;  End: 1469  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003633_01084.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 1 283 2.5e-124 0.7866666666666666

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11349 AmyAc_3 0.0 1 343 106 456
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 1.63e-37 1 346 75 336
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 6.04e-26 9 278 109 347
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 1.09e-23 1 391 76 492
Glycosidase [Carbohydrate transport and metabolism].
cd11316 AmyAc_bac2_AmyA 2.34e-16 1 346 69 403
Alpha amylase catalytic domain found in 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADQ79063.1 1.91e-204 1 447 117 567
BAR51660.1 2.29e-170 1 445 112 561
AEW20328.1 9.21e-170 1 445 112 561
BAR48976.1 1.30e-169 1 445 112 561
AND22072.1 2.45e-169 1 446 112 564

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3DHU_A 8.57e-13 1 244 83 284
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]
1WZA_A 1.27e-12 1 444 81 486
Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
6LGG_A 1.05e-10 1 146 112 239
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]
6LGA_A 1.05e-10 1 146 112 239
Bombyxmori GH13 sucrose hydrolase [Bombyx mori],6LGA_B Bombyx mori GH13 sucrose hydrolase [Bombyx mori],6LGB_A Bombyx mori GH13 sucrose hydrolase complexed with glucose [Bombyx mori],6LGB_B Bombyx mori GH13 sucrose hydrolase complexed with glucose [Bombyx mori],6LGC_A Bombyx mori GH13 sucrose hydrolase complexed with 1-deoxynojirimycin [Bombyx mori],6LGC_B Bombyx mori GH13 sucrose hydrolase complexed with 1-deoxynojirimycin [Bombyx mori],6LGD_A Bombyx mori GH13 sucrose hydrolase complexed with 1,4-dideoxy-1,4-imino-D-arabinitol [Bombyx mori],6LGD_B Bombyx mori GH13 sucrose hydrolase complexed with 1,4-dideoxy-1,4-imino-D-arabinitol [Bombyx mori],6LGE_A Bombyx mori GH13 sucrose hydrolase complexed with acarbose [Bombyx mori],6LGE_B Bombyx mori GH13 sucrose hydrolase complexed with acarbose [Bombyx mori]
7JJT_A 1.26e-10 1 382 106 470
ChainA, Alpha-amylase [Ruminococcus bromii]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P14899 2.83e-10 1 407 103 482
Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
Q9JN46 7.56e-10 1 209 279 448
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2
Q3J3M8 1.07e-09 1 209 297 466
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) OX=272943 GN=glgE PE=3 SV=3
P20845 1.20e-09 1 391 116 488
Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
P14898 3.93e-09 3 386 214 525
Alpha-amylase 2 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyB PE=1 SV=2

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
1.000050 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003633_01084.