CAZyme Information: MGYG000004449_01399

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-245
• CAZyme ID: MGYG000004449_01399
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
286		32387.62	4.7968

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004449	1509316	MAG	Israel	Asia

• Gene Location: Start: 2810; End: 3670 Strand: -

Full Sequence      

MGCDVDLNNVDVVEELTSWSKWYLDLTKVDGFRIDAVKHIRASFFEDWLDELQDYSTKPL
FTVGEYWSGNVESLKNYLEATKNKMCLFDVPLHYNLFNACHSNGHFDMRTIFSNTLVASV
PDKAITFVDNHDTEPGQALESWIDDWFKPHAYSLVLLRKEGIPCIFYGDLYGIPTKGIGN
KMSLLEKLIYARKHFAYGKQTDYFSSSNVIGWVREGDEMHPSSGMAVILTNGSGGCIQMN
VGKKLANSVLYDYLGNLKEPVYVDSDGNGIFYVKDGSISIWTLQES

Enzyme Prediction     

No EC number prediction in MGYG000004449_01399.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	173	7e-73	0.5029239766081871

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09441	PRK09441	1.19e-148	1	281	199	478	cytoplasmic alpha-amylase; Reviewed
cd11318	AmyAc_bac_fung_AmyA	8.81e-115	1	194	197	391	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	2.69e-33	4	196	106	295	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	5.01e-20	2	169	124	293	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.
cd11319	AmyAc_euk_AmyA	1.42e-15	4	168	175	330	Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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
ALU16381.1	4.75e-118	1	281	196	476
QCT72471.1	4.75e-118	1	281	196	476
ARD64410.1	6.73e-118	1	281	196	476
ADO39270.1	6.73e-118	1	281	196	476
AYH41774.1	1.14e-113	1	285	197	480

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HVX_A	1.59e-109	1	286	200	485	BACILLUSSTEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]
4UZU_A	2.12e-109	1	286	198	483	Three-dimensionalstructure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
6AG0_A	8.83e-107	1	286	227	512	TheX-ray Crystallographic Structure of Maltooligosaccharide-forming Amylase from Bacillus stearothermophilus STB04 [Geobacillus stearothermophilus],6AG0_C The X-ray Crystallographic Structure of Maltooligosaccharide-forming Amylase from Bacillus stearothermophilus STB04 [Geobacillus stearothermophilus]
2DIE_A	1.27e-101	1	284	202	485	Alkalinealpha-amylase AmyK from Bacillus sp. KSM-1378 [Bacillus sp. (in: Bacteria)]
1WP6_A	8.14e-100	1	281	202	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P06279	5.80e-109	1	286	234	519	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P19571	1.14e-98	1	281	235	515	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P06278	1.36e-89	1	281	226	509	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P00692	2.03e-89	1	281	228	511	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P26612	1.83e-79	1	285	201	493	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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004449_01399.