CAZyme Information: MGYG000003186_01173

Basic Information

• Species: Gleimia europaea_A
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Gleimia; Gleimia europaea_A
• CAZyme ID: MGYG000003186_01173
• CAZy Family: GH13
• CAZyme Description: Oligo-1,6-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
553	MGYG000003186_1|CGC15	62933.07	4.4024

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003186	1919828	MAG	United States	North America

• Gene Location: Start: 1286044; End: 1287705 Strand: +

Full Sequence      

MTDVQRSDWDQWWRTAVIYQVYPRSFSDSNNDGLGDVRGIINRLDYLKKLGVDAIWMSPH
YPSLQADAGYDVADYFDVNPEYGTLEEFDELIAQAHKRDIKIIIDVVPNHSSDQMKLFRD
ALEAGPNSPERDIYMFRYSEGNRPNNWGSMFGGPAWTAVESLTSNEADRNWWYLHLFAPE
QPDFNWENPKVHEFFKSYLRFWCDRGVDGFRVDVAHGLVKAPGLPDDEIGPDRWSDEALS
FDQTSGPFWDQPGVHDIYREWRSVLDEYGRDRMLVAEAWLTPEREALYVREDEMSQQFNF
NYLKANWDAKRVRAAIDDPIKANAVVGAPVTWVTSNHDVVRATTRYGYEPQIDYDRGIGV
DDPQPDRDLGLARAKGMAVFTMGLPGSMYIYQGEELGLPEVTDLPDESRQDPNWLRTGHQ
VRGRDGCRVPIPWEADAPHFGFGTGDTWLPQPDYFGEFAADIQEDDPASTLNLYRRVLKL
RRELELAKGTVEWVDLGDEKVLAIRNKGVLLVLNMGSKPVNVSDVTAVVASSCDVAINES
GAVVPTNCGAWLR

Enzyme Prediction     

EC	3.2.1.20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	35	400	3.8e-157	0.9972602739726028

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11332	AmyAc_OligoGlu_TS	0.0	11	490	1	479	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), trehalose synthase (also called maltose alpha-D-glucosyltransferase), and related proteins. 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. Trehalose synthase (EC 5.4.99.16) catalyzes the isomerization of maltose to produce trehalulose. 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.
cd11331	AmyAc_OligoGlu_like	1.35e-157	11	483	1	442	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.
cd11333	AmyAc_SI_OligoGlu_DGase	3.36e-157	16	483	3	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.
cd11330	AmyAc_OligoGlu	4.42e-153	12	502	2	472	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.
cd11328	AmyAc_maltase	1.46e-132	12	492	4	470	Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins. Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV01931.1	1.99e-260	1	552	1	553
SDU79129.1	2.22e-254	6	552	2	549
CED90924.1	4.95e-245	6	552	11	565
AMD86436.1	1.83e-243	2	534	6	554
QHO90713.1	3.58e-240	6	552	11	565

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WY4_A	1.52e-96	12	508	7	484	Crystalstructure of alpha-glucosidase mutant E271Q in complex with maltose [Halomonas sp. H11],3WY4_B Crystal structure of alpha-glucosidase mutant E271Q in complex with maltose [Halomonas sp. H11]
3WY1_A	1.52e-96	12	508	7	484	Crystalstructure of alpha-glucosidase [Halomonas sp. H11],3WY1_B Crystal structure of alpha-glucosidase [Halomonas sp. H11],3WY2_A Crystal structure of alpha-glucosidase in complex with glucose [Halomonas sp. H11],3WY2_B Crystal structure of alpha-glucosidase in complex with glucose [Halomonas sp. H11]
3WY3_A	8.39e-96	12	508	7	484	Crystalstructure of alpha-glucosidase mutant D202N in complex with glucose and glycerol [Halomonas sp. H11],3WY3_B Crystal structure of alpha-glucosidase mutant D202N in complex with glucose and glycerol [Halomonas sp. H11]
6AAV_A	3.85e-91	12	519	12	502	Crystalstructure of alpha-glucosyl transfer enzyme, XgtA at 1.72 angstrom resolution [Xanthomonas campestris],6AAV_B Crystal structure of alpha-glucosyl transfer enzyme, XgtA at 1.72 angstrom resolution [Xanthomonas campestris]
2PWG_A	2.06e-90	12	519	5	512	ChainA, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWG_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWH_A Chain A, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWH_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29094	9.59e-94	12	506	5	510	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
Q9K8U9	2.54e-89	11	505	4	496	Oligo-1,6-glucosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=malL PE=3 SV=1
Q9Z3R8	1.07e-88	12	506	17	506	Probable alpha-glucosidase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=aglA PE=3 SV=2
P39795	1.39e-88	12	514	8	507	Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2
P21332	5.81e-86	11	486	4	476	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000040	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003186_01173.