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CAZyme Information: MGYG000004792_01788

You are here: Home > Sequence: MGYG000004792_01788

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; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus;
CAZyme ID MGYG000004792_01788
CAZy Family GH70
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1576 173425.39 5.1288
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004792 1933522 MAG China Asia
Gene Location Start: 4510;  End: 9240  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH70 775 1564 2.6e-278 0.9838107098381071

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02324 Glyco_hydro_70 0.0 775 1563 1 790
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 3.29e-14 1353 1437 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 4.43e-14 1353 1451 21 122
cytoplasmic alpha-amylase; Reviewed
cd11318 AmyAc_bac_fung_AmyA 9.37e-14 1353 1451 19 120
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 1.38e-12 921 1299 198 479
cytoplasmic alpha-amylase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AAU08014.2 0.0 1 1560 1 1610
QLL76139.1 0.0 1 1560 1 1607
QDK48457.1 0.0 1 1560 1 1610
AAU08003.2 0.0 1 1560 1 1611
ASA47882.1 0.0 9 1560 1 1603

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7DT1_A 0.0 688 1573 154 1045
ChainA, Dextransucrase [Limosilactobacillus fermentum],7DT1_B Chain B, Dextransucrase [Limosilactobacillus fermentum]
5JBE_A 0.0 722 1560 1 850
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 0.0 722 1560 1 850
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 0.0 716 1560 23 878
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 0.0 701 1570 29 880
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
P13470 2.44e-157 729 1538 249 1063
Glucosyltransferase-SI OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfC PE=1 SV=2
P08987 2.41e-155 688 1570 170 1067
Glucosyltransferase-I OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfB PE=3 SV=3
P11001 1.04e-149 729 1528 223 1030
Glucosyltransferase-I OS=Streptococcus downei OX=1317 GN=gtfI PE=3 SV=1
P27470 8.94e-149 729 1528 217 1024
Glucosyltransferase-I OS=Streptococcus downei OX=1317 PE=3 SV=1
P49331 2.06e-137 726 1563 232 1089
Glucosyltransferase-S OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfD PE=3 SV=3

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.002570 0.996054 0.000540 0.000327 0.000262 0.000214

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004792_01788.