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CAZyme Information: MGYG000002319_01119

You are here: Home > Sequence: MGYG000002319_01119

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 Limosilactobacillus mucosae
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus mucosae
CAZyme ID MGYG000002319_01119
CAZy Family GH70
CAZyme Description Glucosyltransferase-SI
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1111 125270.03 4.8242
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002319 2369669 Isolate not provided not provided
Gene Location Start: 50999;  End: 54334  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH70 308 1105 1.4e-294 0.9800747198007472

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02324 Glyco_hydro_70 0.0 308 1102 1 786
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.
cd11314 AmyAc_arch_bac_plant_AmyA 1.26e-14 897 981 17 94
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.
PRK09441 PRK09441 2.42e-14 456 843 189 479
cytoplasmic alpha-amylase; Reviewed
cd11318 AmyAc_bac_fung_AmyA 1.46e-13 897 996 19 123
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 1.80e-13 897 994 21 121
cytoplasmic alpha-amylase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASA47904.1 0.0 231 1111 276 1149
ASA47860.1 0.0 233 1108 1102 1979
ASA47801.1 0.0 239 1107 19 877
ASA47869.1 0.0 239 1107 19 877
ASA47877.1 0.0 239 1107 19 877

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7DT1_A 0.0 233 1108 165 1036
ChainA, Dextransucrase [Limosilactobacillus fermentum],7DT1_B Chain B, Dextransucrase [Limosilactobacillus fermentum]
5JBE_A 0.0 255 1108 1 854
4,6-alpha-glucanotransferaseGTFB from Lactobacillus reuteri 121 complexed with an isomalto-maltopentasaccharide [Limosilactobacillus reuteri],5JBE_B 4,6-alpha-glucanotransferase GTFB from Lactobacillus reuteri 121 complexed with an isomalto-maltopentasaccharide [Limosilactobacillus reuteri]
5JBF_A 0.0 255 1108 1 854
4,6-alpha-glucanotransferaseGTFB (D1015N mutant) from Lactobacillus reuteri 121 complexed with maltopentaose [Limosilactobacillus reuteri],5JBF_B 4,6-alpha-glucanotransferase GTFB (D1015N mutant) from Lactobacillus reuteri 121 complexed with maltopentaose [Limosilactobacillus reuteri]
5JBD_A 0.0 231 1109 5 883
4,6-alpha-glucanotransferaseGTFB from Lactobacillus reuteri 121 [Limosilactobacillus reuteri],5JBD_B 4,6-alpha-glucanotransferase GTFB from Lactobacillus reuteri 121 [Limosilactobacillus reuteri]
7P38_A 0.0 233 1108 26 874
ChainA, Dextransucrase [Limosilactobacillus reuteri],7P38_B Chain B, Dextransucrase [Limosilactobacillus reuteri],7P39_A Chain A, Dextransucrase [Limosilactobacillus reuteri],7P39_B Chain B, Dextransucrase [Limosilactobacillus reuteri]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P08987 9.38e-169 262 1102 223 1056
Glucosyltransferase-I OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfB PE=3 SV=3
P13470 1.29e-165 262 1107 249 1084
Glucosyltransferase-SI OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfC PE=1 SV=2
P11001 3.16e-153 262 1099 223 1056
Glucosyltransferase-I OS=Streptococcus downei OX=1317 GN=gtfI PE=3 SV=1
P49331 3.23e-150 268 1110 241 1092
Glucosyltransferase-S OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfD PE=3 SV=3
P27470 1.02e-149 262 1111 217 1059
Glucosyltransferase-I OS=Streptococcus downei OX=1317 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
1.000073 0.000004 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002319_01119.