CAZyme Information: MGYG000002395_01732

Basic Information

• Species: Bifidobacterium adolescentis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium adolescentis
• CAZyme ID: MGYG000002395_01732
• CAZy Family: GH13
• CAZyme Description: Oligo-1,6-glucosidase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
543	MGYG000002395_1|CGC29	60975.32	5.1774

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002395	2173720	Isolate	China	Asia

• Gene Location: Start: 2047391; End: 2049022 Strand: +

Full Sequence      

MLSPAKHPHPKWLADAIFYEIYPQSFVDSNGDGIGDIPGITLKLDYIKDLGCNAIWLNPC
FDSPFKDAGYDVRDYKKVASRYGTNDDLIALFDAAHRRDMHVILDLVPGHTSEEHEWFHR
SCKVERNNYSDRYIWTDSWISGGDGLPFIGGESPRNGTYILNFFKCQPALNYGFAHPERS
WQKPALGPDAKATCDAMVDVMRFWLSRGADGFRVDMADSLVKKDDEGKPYTIRTWQYMFA
RIRPAFPEAAFVSEWGRPEESMAAGFDMDFYLDWRWDGVPNGYNMLLRNVDDPLSRKGDK
SYFNADSGTPISEFLDEYEPRLREAETADGNFNFITCNHDTARVAPRLSQREIALAYCTL
FAMPGVPFLYYGDEIGMRYRALPGKEGGYVRTGSRTPMQWGANDASGALHVSDSAESDTR
AGDVTGGSYLPADPSADAPTVAAQQADAESLWHTVRSILHVKRECDALRSGATFHAIERD
RVFVFKRSTHLQKLIIAVNPSRDCKALQLPDGSYRTIFSIGENEISGTSLRLGLQSFAIL
EAE

Enzyme Prediction     

No EC number prediction in MGYG000002395_01732.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	35	378	1.7e-69	0.9264214046822743

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11348	AmyAc_2	0.0	17	460	1	428	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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 catalytic triad (DED) is not present here. 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	5.20e-94	15	464	2	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.
cd11331	AmyAc_OligoGlu_like	2.21e-90	11	471	1	449	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.
cd11316	AmyAc_bac2_AmyA	4.93e-86	16	471	1	403	Alpha amylase catalytic domain found in bacterial 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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.
cd11334	AmyAc_TreS	1.65e-83	12	461	1	446	Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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
AJE06700.1	0.0	1	543	1	543
AZH72122.1	0.0	1	543	1	543
AXR42390.1	0.0	1	543	1	543
AII76855.1	0.0	1	543	1	543
QHB63493.1	0.0	1	543	1	543

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4MB1_A	4.99e-65	11	510	3	523	TheStructure of MalL mutant enzyme G202P from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]
4M56_A	4.99e-65	11	510	3	523	TheStructure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],4M56_B The Structure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
7LV6_B	8.36e-65	11	510	28	548	ChainB, Oligo-1,6-glucosidase 1 [Bacillus subtilis subsp. subtilis str. 168]
5WCZ_A	8.36e-65	11	510	28	548	CrystalStructure of Wild-Type MalL from Bacillus subtilis with TS analogue 1-deoxynojirimycin [Bacillus subtilis subsp. subtilis str. 168],5WCZ_B Crystal Structure of Wild-Type MalL from Bacillus subtilis with TS analogue 1-deoxynojirimycin [Bacillus subtilis subsp. subtilis str. 168]
4M8U_A	9.49e-65	11	510	3	523	TheStructure of MalL mutant enzyme V200A from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q45101	1.72e-64	11	529	3	540	Oligo-1,6-glucosidase OS=Weizmannia coagulans OX=1398 GN=malL PE=3 SV=1
O06994	2.73e-64	11	510	3	523	Oligo-1,6-glucosidase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=malL PE=1 SV=1
A0R6E0	2.81e-60	12	471	35	493	Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS PE=1 SV=1
P29093	3.83e-58	11	496	3	508	Oligo-1,6-glucosidase OS=Bacillus sp. (strain F5) OX=268806 GN=malL PE=1 SV=2
P9WQ19	2.31e-57	10	472	41	502	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treS 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
1.000057	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002395_01732.