logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002469_00409

You are here: Home > Sequence: MGYG000002469_00409

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 Bifidobacterium breve
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium breve
CAZyme ID MGYG000002469_00409
CAZy Family GH13
CAZyme Description Amylosucrase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
150 17180.52 8.0119
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002469 2422684 Isolate not provided not provided
Gene Location Start: 484548;  End: 485000  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002469_00409.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11324 AmyAc_Amylosucrase 8.85e-71 2 133 22 157
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.
smart00642 Aamy 2.50e-13 53 133 3 91
Alpha-amylase domain.
cd00551 AmyAc_family 3.22e-12 55 133 18 97
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.
PRK10785 PRK10785 4.74e-12 57 133 174 247
maltodextrin glucosidase; Provisional
COG0366 AmyA 6.90e-11 59 133 26 98
Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ABE95061.1 6.23e-107 1 150 1 150
QFV13670.1 1.76e-106 1 150 31 180
AUD82405.1 1.79e-106 1 150 1 150
AHJ15093.1 1.53e-103 1 150 44 193
AEF27348.1 1.53e-103 1 150 44 193

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4AYS_A 3.68e-34 2 133 44 177
TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans]
3UCQ_A 1.33e-33 13 133 62 182
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]
4FLS_A 9.21e-31 2 133 49 184
Crystalstructure of Amylosucrase inactive double mutant F290K-E328Q from Neisseria polysaccharea in complex with sucrose. [Neisseria polysaccharea]
4FLR_A 9.21e-31 2 133 49 184
Crystalstructure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea [Neisseria polysaccharea]
4FLQ_A 9.21e-31 2 133 49 184
Crystalstructure of Amylosucrase double mutant A289P-F290I 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
Q9ZEU2 5.14e-30 2 133 57 192
Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
Q84HD6 1.80e-29 2 133 57 192
Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
P0CW40 3.73e-09 36 139 9 115
Oligo-1,6-glucosidase IMA3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA3 PE=1 SV=1
Q08295 3.73e-09 36 139 9 115
Oligo-1,6-glucosidase IMA2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA2 PE=2 SV=1
P0CW41 3.73e-09 36 139 9 115
Oligo-1,6-glucosidase IMA4 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA4 PE=3 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
1.000051 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002469_00409.