CAZyme Information: MGYG000000756_01436

Basic Information

• Species: Bifidobacterium sp002742445
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium sp002742445
• CAZyme ID: MGYG000000756_01436
• CAZy Family: GH13
• CAZyme Description: Oligo-1,6-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
403	MGYG000000756_35|CGC1	45659.93	4.5527

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000756	1963853	MAG	Bangladesh	Asia

• Gene Location: Start: 181; End: 1392 Strand: +

Full Sequence      

MYRMMNWWMDRGIDGFRMDVITLISKYLDSHGRLPGEVDSELSEGEIGEEGYTNASPFCS
DGPRLDEFLAEMRREVFEGREGYMNVGEAPGITPERNEFITNPAHKELDMLFLFDHVSVD
QSPESKWDTHAFAPKKLQDRMSRQQEAVRNAGWASLFFCNHDQPRVVSRWGDDTDRESRE
LSAKAFGMLLHMHRGTPYIYEGEELGMTNAHFTRLDQYRDLEAVNAYRQRVEEAKCQSPE
SMMAALALIGRDNSRTPMQWDASRYAGFTAPDAATEPWIGVNPNHVEINAAEEFDDPDSV
YTFYKKLIAMRHNNATVAVGEWNLLDADDEQVYAFTRTGGDDTILVVVNLTGRTARVPAE
VARLLGNGVDESQVLLSTYDAVHGVRSIARGELARWEGVVIQL

Enzyme Prediction     

No EC number prediction in MGYG000000756_01436.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	209	6.7e-62	0.5558739255014327

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11333	AmyAc_SI_OligoGlu_DGase	9.88e-120	1	313	175	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.
PRK10933	PRK10933	7.20e-97	7	383	188	532	trehalose-6-phosphate hydrolase; Provisional
COG0366	AmyA	3.87e-62	1	371	180	504	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	4.17e-48	1	211	154	332	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
cd11331	AmyAc_OligoGlu_like	2.21e-43	1	320	179	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAJ72120.1	1.13e-286	2	403	194	595
BCB69637.1	1.75e-286	2	403	206	607
AIZ15253.1	5.82e-285	2	403	206	607
BAR02544.1	1.06e-280	2	403	206	607
QSG87674.1	3.57e-274	2	403	206	606

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5DO8_A	1.09e-95	2	403	180	552	1.8Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e],5DO8_B 1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e],5DO8_C 1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e]
1UOK_A	3.30e-95	2	403	182	557	CrystalStructure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus]
4MB1_A	2.08e-90	2	385	182	559	TheStructure of MalL mutant enzyme G202P from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]
4M56_A	2.94e-90	2	385	182	559	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]
5WCZ_A	5.54e-90	2	385	207	584	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29094	2.73e-101	2	403	182	559	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
Q9K8U9	2.25e-96	2	380	182	536	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
P21332	1.81e-94	2	403	182	557	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
O06994	1.61e-89	2	385	182	559	Oligo-1,6-glucosidase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=malL PE=1 SV=1
P43473	8.26e-85	2	373	184	542	Alpha-glucosidase OS=Pediococcus pentosaceus OX=1255 GN=agl PE=3 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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000756_01436.