CAZyme Information: MGYG000000083_03483

Basic Information

• Species: Peribacillus simplex
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_B; DSM-1321; Peribacillus; Peribacillus simplex
• CAZyme ID: MGYG000000083_03483
• CAZy Family: GH13
• CAZyme Description: Glucan 1,4-alpha-maltohexaosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
531		61570.72	4.9375

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000083	5860218	Isolate	United Kingdom	Europe

• Gene Location: Start: 539599; End: 541194 Strand: +

Full Sequence      

MNLNQEGCSLVYHLNLGGKDFHYYFIRSYSFTFFKNRSVSGGERMKRNHTMMQFFEWHLE
ADGSHWDRLKYAASKLKDIGIDCVWLPPVTKGQSVGDNGYGIYDGYDLGEFDQKGTVRTK
YGTKDELLQAIDTCHNYGLCVYIDLVMNHKAGADGTEKFEVIEVNPDNRMEDISEPFEME
GWTKFDFPGRKNKYSDFKWNHNHFNGTDYDAENDKMSVYRITGENKHWNQHVIDEFGNYD
YLMFANIDYSLPEVRQEMISWGKWMVDTLKCDGFRLDAVKHIDYEFINEFLQELIPYTKE
HFFMVGEFWKADVKACQTYLEQTNHDLNLFDVSLHYKFHEASKAGTDFDLSTIFDDTLVQ
TNPAQAVTFVDNHDSQPHESLESWVKDWFKPSAYALTLLRLCGYPCVFYGDYYGIGGPSP
VPGKKDILDRLLYARYEKAYGEQTDYFDDPNTIGWVRHGVKELEGSGCAVIISNGDHNSE
KRMFVGEHRAGEIWIDLTCHRDDHITIEEDGFATFPVHGKSVSVWALNNPL

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	75	415	1.3e-151	0.9970760233918129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11318	AmyAc_bac_fung_AmyA	0.0	48	435	1	389	Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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.
PRK09441	PRK09441	0.0	47	526	2	479	cytoplasmic alpha-amylase; Reviewed
cd11314	AmyAc_arch_bac_plant_AmyA	2.69e-47	51	435	2	291	Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 AmyA from bacteria, archaea, water fleas, and plants. 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.
pfam00128	Alpha-amylase	1.20e-29	67	420	8	334	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.
COG0366	AmyA	3.55e-28	67	455	33	398	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASS94628.1	0.0	45	531	1	487
AZV61945.1	0.0	45	531	1	487
QYF83153.1	0.0	45	531	1	487
QOS91766.1	0.0	45	531	1	487
QNK49642.1	0.0	45	531	1	487

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2GJP_A	4.04e-180	45	525	3	482	ChainA, alpha-amylase [Sutcliffiella halmapala],2GJR_A Chain A, alpha-amylase [Sutcliffiella halmapala]
1W9X_A	7.06e-180	48	525	2	478	ChainA, Alpha Amylase [Sutcliffiella halmapala]
1WP6_A	5.33e-178	48	525	6	482	Crystalstructure of maltohexaose-producing amylase from alkalophilic Bacillus sp.707. [Bacillus sp. 707],1WPC_A Crystal structure of maltohexaose-producing amylase complexed with pseudo-maltononaose [Bacillus sp. 707],2D3L_A Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltopentaose. [Bacillus sp. 707],2D3N_A Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose [Bacillus sp. 707]
1HVX_A	1.38e-175	48	525	5	480	BACILLUSSTEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]
2DIE_A	5.68e-175	48	525	6	482	Alkalinealpha-amylase AmyK from Bacillus sp. KSM-1378 [Bacillus sp. (in: Bacteria)]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P19571	9.03e-177	48	525	39	515	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P06279	5.91e-175	48	525	39	514	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P00692	6.13e-166	48	525	33	511	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P06278	5.57e-161	48	525	33	509	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P26613	4.27e-137	47	529	2	493	Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 SV=3

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
1.000074	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000083_03483.