CAZyme Information: MGYG000003789_01763

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus
• CAZyme ID: MGYG000003789_01763
• CAZy Family: GH13
• CAZyme Description: Glucan 1,4-alpha-maltohexaosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
288		33321.35	4.3843

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003789	1827958	MAG	Canada	North America

• Gene Location: Start: 38; End: 904 Strand: +

Full Sequence      

MNCDIDHNHPEVREEIFKWVDWFIMETKVDGFRYDALKHISGDFIYELSKHIYDNMGENK
FYLFGEFWQYNTGAIENYLQNSDYKIDLFDVPLHFHMAEASKSMGGYDMRKIFDGTVVKE
FPAQAVTFVDNHDSQPGQALDSWVEDWFKEIAYALILFRKDGYPCLFAGDYYGLIGPVKK
DPLKDMLDKMMAVRKAYNYGEEDDYFDHPSVIGWVRRGDDDHKPLAVLISIQDMAEKQMF
VGESEAGATYVDLSGKNEEITIDENGNGVFTVGPGQVTYWTNKESLEK

Enzyme Prediction     

No EC number prediction in MGYG000003789_01763.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	173	1.5e-67	0.5

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09441	PRK09441	1.11e-136	1	280	199	478	cytoplasmic alpha-amylase; Reviewed
cd11318	AmyAc_bac_fung_AmyA	4.42e-104	1	195	197	390	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.
cd11314	AmyAc_arch_bac_plant_AmyA	1.79e-25	4	196	106	293	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.
cd11339	AmyAc_bac_CMD_like_2	9.64e-16	3	176	125	299	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.
COG0366	AmyA	6.56e-12	4	240	168	432	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACV29558.1	2.45e-176	1	286	198	483
QQB62236.1	3.11e-157	1	285	197	481
QQN55281.1	6.26e-157	1	285	197	481
QUE85074.1	5.80e-103	1	285	200	486
QPI68799.1	5.98e-103	1	284	201	486

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1WP6_A	1.01e-83	1	283	202	485	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]
6GXV_A	3.88e-83	1	283	200	484	Amylasein complex with acarbose [Alicyclobacillus sp.],6GXV_B Amylase in complex with acarbose [Alicyclobacillus sp.],6GYA_A Amylase in complex with branched ligand [Alicyclobacillus sp.],6GYA_B Amylase in complex with branched ligand [Alicyclobacillus sp.],6GYA_C Amylase in complex with branched ligand [Alicyclobacillus sp.],6GYA_D Amylase in complex with branched ligand [Alicyclobacillus sp.]
1BPL_B	5.46e-83	1	283	8	294	Glycosyltransferase[Bacillus licheniformis]
1OB0_A	2.36e-81	1	283	197	483	Kineticstabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface [Bacillus licheniformis]
1BLI_A	2.36e-81	1	283	197	483	BacillusLicheniformis Alpha-Amylase [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P19571	1.30e-82	1	283	235	518	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P06278	1.52e-79	1	283	226	512	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P00692	1.77e-78	1	283	228	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P06279	1.96e-75	1	285	234	519	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P26612	3.68e-56	1	286	201	495	Cytoplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=amyA PE=1 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
1.000037	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003789_01763.