logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003427_02594

You are here: Home > Sequence: MGYG000003427_02594

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 HGM12587 sp900766915
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; HGM12587; HGM12587 sp900766915
CAZyme ID MGYG000003427_02594
CAZy Family GH13
CAZyme Description Amylosucrase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
617 MGYG000003427_353|CGC1 72224.47 5.1949
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003427 3377258 MAG Fiji Oceania
Gene Location Start: 59671;  End: 61524  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003427_02594.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 80 477 2.1e-168 0.9975

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11324 AmyAc_Amylosucrase 0.0 3 534 1 536
Alpha amylase catalytic domain found in Amylosucrase. Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. 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.
cd11334 AmyAc_TreS 4.83e-64 81 506 24 398
Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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.
cd11356 AmyAc_Sucrose_phosphorylase-like_1 1.04e-60 95 538 35 446
Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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.
cd11343 AmyAc_Sucrose_phosphorylase-like 5.00e-55 98 538 36 443
Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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 1.95e-49 81 577 26 492
Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWY96820.1 0.0 5 610 8 612
QEK18306.1 0.0 5 609 8 611
CBL26996.1 6.48e-317 2 609 11 617
QRT49301.1 9.93e-313 5 610 6 610
QDW74185.1 3.74e-312 10 610 10 609

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7ESH_A 4.81e-138 3 571 29 601
ChainA, amylosucrase [Calidithermus timidus DSM 17022],7ESH_B Chain B, amylosucrase [Calidithermus timidus DSM 17022],7ESH_C Chain C, amylosucrase [Calidithermus timidus DSM 17022],7ESH_D Chain D, amylosucrase [Calidithermus timidus DSM 17022]
3UCQ_A 7.15e-134 3 608 28 648
Crystalstructure of amylosucrase from Deinococcus geothermalis [Deinococcus geothermalis DSM 11300],3UER_A Crystal structure of amylosucrase from Deinococcus geothermalis in complex with turanose [Deinococcus geothermalis DSM 11300]
4AYS_A 3.61e-132 3 608 23 644
TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans]
5N7J_A 7.96e-132 7 609 32 626
Crystalstructure of Neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides [Neisseria polysaccharea]
4FLR_A 4.45e-131 7 609 32 626
Crystalstructure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea [Neisseria polysaccharea]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q84HD6 1.22e-129 7 609 40 634
Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
Q9ZEU2 4.82e-129 7 609 40 634
Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
P76041 2.49e-42 24 609 11 559
Glucosylglycerate phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=ycjM PE=1 SV=2
A0R6E0 1.35e-41 60 518 32 447
Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS PE=1 SV=1
G0GBS4 2.33e-41 101 569 92 527
Glucosylglycerate phosphorylase OS=Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203) OX=869211 GN=Spith_0877 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
1.000073 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003427_02594.