dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Lactococcus garvieae

Lineage

Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Lactococcus; Lactococcus garvieae

CAZyme ID

MGYG000000582_00630

CAZy Family

GH13

CAZyme Description

Glucan 1,6-alpha-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
542	MGYG000000582_4\|CGC3	62961.87	4.6195

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000582	2064828	MAG	Madagascar	Africa

Gene Location

Start: 137736; End: 139364 Strand: -

Enzyme Prediction help

EC	5.4.99.11	3.2.1.10	3.2.1.20	3.2.1.70	3.2.1.-	2.4.1.-

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	29	363	5.9e-155	0.994269340974212

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10933	PRK10933	0.0	1	536	2	545	trehalose-6-phosphate hydrolase; Provisional
cd11333	AmyAc_SI_OligoGlu_DGase	0.0	8	461	1	428	Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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.
TIGR02403	trehalose_treC	0.0	6	541	1	543	alpha,alpha-phosphotrehalase. Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.
cd11331	AmyAc_OligoGlu_like	6.60e-161	6	463	2	444	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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	2.73e-157	11	511	2	496	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
QSQ99678.1	1	542	1	542
BAK60739.1	1	542	1	542
BAK58771.1	1	542	1	542
QSQ97675.1	1	542	1	542
QSR01505.1	1	542	1	542

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4AIE_A	1.04e-264	5	541	5	539	Structureof glucan-1,6-alpha-glucosidase from Lactobacillus acidophilus NCFM [Lactobacillus acidophilus NCFM]
2ZIC_A	2.90e-246	3	541	2	535	ChainA, Dextran glucosidase [unidentified]
4WLC_A	6.43e-246	3	541	2	535	Structureof dextran glucosidase with glucose [Streptococcus mutans UA159],4XB3_A Structure of dextran glucosidase [Streptococcus mutans UA159]
2ZID_A	8.28e-246	3	541	2	535	ChainA, Dextran glucosidase [unidentified]
1UOK_A	1.08e-230	3	542	2	558	CrystalStructure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54796	1.44e-258	3	541	2	534	Glucan 1,6-alpha-glucosidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=dexB PE=3 SV=2
Q99040	1.23e-245	3	541	2	535	Glucan 1,6-alpha-glucosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=dexB PE=1 SV=2
Q59905	7.57e-240	3	541	2	535	Glucan 1,6-alpha-glucosidase OS=Streptococcus dysgalactiae subsp. equisimilis OX=119602 GN=dexB PE=3 SV=1
P21332	5.90e-230	3	542	2	558	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
P29094	1.97e-224	6	542	5	560	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL 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
1.000052	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000582_00630.

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