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CAZyme Information: MGYG000000096_01544

You are here: Home > Sequence: MGYG000000096_01544

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 Leuconostoc pseudomesenteroides
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Leuconostoc; Leuconostoc pseudomesenteroides
CAZyme ID MGYG000000096_01544
CAZy Family GH70
CAZyme Description Glucosyltransferase-SI
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
458 MGYG000000096_4|CGC3 50672.33 4.2153
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000096 2296803 Isolate Canada North America
Gene Location Start: 68825;  End: 70201  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.5 2.4.1.- 2.4.1.140

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH70 1 453 1.7e-206 0.5354919053549191

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02324 Glyco_hydro_70 0.0 1 456 351 786
Glycosyl hydrolase family 70. Members of this family belong to glycosyl hydrolase family 70 Glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) catalyze the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules, EC:2.4.1.5. This family roughly corresponds to the N-terminal catalytic domain of the enzyme. Members of this family also contain the Putative cell wall binding domain pfam01473, which corresponds with the C-terminal glucan-binding domain.
cd11318 AmyAc_bac_fung_AmyA 7.96e-12 235 317 22 103
Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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.
PRK09441 PRK09441 1.89e-09 246 316 35 104
cytoplasmic alpha-amylase; Reviewed
cd11314 AmyAc_arch_bac_plant_AmyA 3.14e-07 272 316 50 90
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.
cd00551 AmyAc_family 3.49e-06 242 314 34 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWV37885.1 2.66e-292 1 458 2402 2859
BAX70498.1 1.99e-286 1 458 2394 2851
API71911.1 2.58e-286 1 458 2412 2869
QHM56159.1 6.82e-284 1 458 2384 2841
ABJ61965.1 1.93e-283 1 458 2364 2821

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3TTO_A 1.08e-257 1 453 622 1073
Crystalstructure of Leuconostoc mesenteroides NRRL B-1299 N-terminally truncated dextransucrase DSR-E in triclinic form [Leuconostoc mesenteroides],3TTO_B Crystal structure of Leuconostoc mesenteroides NRRL B-1299 N-terminally truncated dextransucrase DSR-E in triclinic form [Leuconostoc mesenteroides],3TTO_C Crystal structure of Leuconostoc mesenteroides NRRL B-1299 N-terminally truncated dextransucrase DSR-E in triclinic form [Leuconostoc mesenteroides],3TTO_D Crystal structure of Leuconostoc mesenteroides NRRL B-1299 N-terminally truncated dextransucrase DSR-E in triclinic form [Leuconostoc mesenteroides],3TTQ_A Crystal structure of Leuconostoc mesenteroides NRRL B-1299 N-terminally truncated dextransucrase DSR-E in orthorhombic apo-form at 1.9 angstrom resolution [Leuconostoc mesenteroides]
4TTU_A 1.74e-256 1 453 622 1073
N-terminallytruncated dextransucrase DSR-E from Leuconostoc mesenteroides NRRL B-1299 in complex with isomaltotriose [Leuconostoc mesenteroides],4TVC_A N-terminally truncated dextransucrase DSR-E from Leuconostoc mesenteroides NRRL B-1299 in complex with gluco-oligosaccharides [Leuconostoc mesenteroides]
4TVD_A 2.79e-255 1 453 622 1073
N-terminallytruncated dextransucrase DSR-E from Leuconostoc mesenteroides NRRL B-1299 in complex with D-glucose [Leuconostoc mesenteroides subsp. mesenteroides]
3KLK_A 2.77e-171 1 456 454 889
Crystalstructure of Lactobacillus reuteri N-terminally truncated glucansucrase GTF180 in triclinic apo- form [Limosilactobacillus reuteri],4AYG_A Lactobacillus reuteri N-terminally truncated glucansucrase GTF180 in orthorhombic apo-form [Limosilactobacillus reuteri],4AYG_B Lactobacillus reuteri N-terminally truncated glucansucrase GTF180 in orthorhombic apo-form [Limosilactobacillus reuteri]
3HZ3_A 2.77e-171 1 456 454 889
Lactobacillusreuteri N-terminally truncated glucansucrase GTF180(D1025N)-sucrose complex [Limosilactobacillus reuteri]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P13470 8.70e-136 1 453 647 1078
Glucosyltransferase-SI OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfC PE=1 SV=2
P08987 1.17e-134 1 448 621 1047
Glucosyltransferase-I OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfB PE=3 SV=3
P49331 2.68e-128 1 448 643 1078
Glucosyltransferase-S OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfD PE=3 SV=3
P27470 2.92e-126 1 450 617 1046
Glucosyltransferase-I OS=Streptococcus downei OX=1317 PE=3 SV=1
P11001 4.24e-126 1 448 623 1050
Glucosyltransferase-I OS=Streptococcus downei OX=1317 GN=gtfI 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
1.000074 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000096_01544.