CAZyme Information: MGYG000003710_00439

Basic Information

• Species: Loigolactobacillus coryniformis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Loigolactobacillus; Loigolactobacillus coryniformis
• CAZyme ID: MGYG000003710_00439
• CAZy Family: GH13
• CAZyme Description: Oligo-1,6-glucosidase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
407	MGYG000003710_24|CGC1	47859.88	6.4452

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003710	2331695	MAG	Russia	Europe

• Gene Location: Start: 13553; End: 14776 Strand: -

Full Sequence      

MPERQQYYLHYYAKEQPDLNWENPLVRQAIYDMMRFWKAQGVDGWRMDVISSISKDQHFT
DYPDKLNRPYVLSDQNNGPRLHEFIQEMNREVLAPFNMMSVGEAPGATAANVRKFVDPER
KELDMVFSFEHMRADRKAGGVNGKWDYDHFDLLKLKDSLTKWQDNLRDHGWNALYFENHD
RARIVSRWGNDQKYRYQSATAFATVLHGMQGTPFVYQGEEIGMTNATFALADHEDIEITT
NYRQYVEQDQTMTATEFLAAAQKLSRDHARTPMQWDTSANAGFTIGRPWFQLNPNYRQIN
VATDRQQHASIFKYYQQLIQLRHQFPILTTGRYQLELPTDQQLFVYRRVTAEQSWLIVAN
LSAQIVPITRLAELVTTEFVFKLKNNTHRCALDENIQPYEAFILELI

Enzyme Prediction     

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

Family	Start	End	Evalue	family coverage
GH13	2	225	3.8e-85	0.6361031518624641

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11333	AmyAc_SI_OligoGlu_DGase	4.17e-157	2	324	147	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	1.59e-139	2	406	147	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.
PRK10933	PRK10933	1.70e-125	3	401	155	545	trehalose-6-phosphate hydrolase; Provisional
COG0366	AmyA	8.93e-73	2	369	152	491	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	7.18e-71	3	226	127	331	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATO55963.1	2.82e-307	1	407	153	559
ATO44276.1	2.82e-307	1	407	153	559
QEA53343.1	4.66e-306	1	407	153	559
ASZ34947.1	9.91e-185	2	405	154	556
ATF26375.1	3.87e-182	4	405	156	553

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4M8U_A	8.03e-142	6	401	157	554	TheStructure of MalL mutant enzyme V200A from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]
4M56_A	9.43e-141	6	401	157	555	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	1.02e-140	6	401	182	580	ChainB, Oligo-1,6-glucosidase 1 [Bacillus subtilis subsp. subtilis str. 168]
4MB1_A	1.33e-140	6	401	157	555	TheStructure of MalL mutant enzyme G202P from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]
5WCZ_A	2.04e-140	6	401	182	580	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
Q45101	1.02e-143	6	362	157	514	Oligo-1,6-glucosidase OS=Weizmannia coagulans OX=1398 GN=malL PE=3 SV=1
O06994	5.16e-140	6	401	157	555	Oligo-1,6-glucosidase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=malL PE=1 SV=1
P29093	5.79e-121	6	348	156	499	Oligo-1,6-glucosidase OS=Bacillus sp. (strain F5) OX=268806 GN=malL PE=1 SV=2
P29094	1.81e-118	6	406	157	559	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
Q9K8U9	1.26e-115	6	401	157	553	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

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
1.000041	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003710_00439.