CAZyme Information: MGYG000000223_00228

Basic Information

• Species: NSJ-61 sp003433845
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; NSJ-61; NSJ-61 sp003433845
• CAZyme ID: MGYG000000223_00228
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
491	MGYG000000223_1|CGC6	56851.66	4.5116

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000223	4367631	Isolate	China	Asia

• Gene Location: Start: 238986; End: 240461 Strand: -

Full Sequence      

MTKTNGVILQYFEWYLPNQPHLWKLLKQDAKHLADIGITAVWIPPAYKGAAGNQDVGYGV
YDLYDLGEFPQKGSIETKYGTKEELLDAINALHMYDIDVYADIVFDHKMGADATEQILAV
SVDPRDREEITSNEETIEAWTKFTFPGRNGKYSDYIWNWDDFDGIDYDQATKENRIFRFY
GKDWDQQVDGEYQNYDYLMGADIDFQNPDVIQELNRWGSWFVDTTKIDGFRMDAVKHIHF
GFYKNWLEKLRKDTGKELFSVGEYWSGDINKLIHYMQVDDYMMSLFDVPLHYHFYDASRS
NGHYDMSKLLDGTLVSYDEFKAVTFVDNHDTQIGQSLESWVLDWFKPMAYAMILLRQQGY
PCIFYGDYYGIPHNQISGLRDTLDILLYLRKNLAYGIQHDYFDDPHVVGFTRSGDAKHTG
GLAVLLSDQMGGQKKMCIDTTYAHVCYRDCLHPEKDSVILDENGCGNFLVDSGSLSIYIP
DTDGFFDKKPV

Enzyme Prediction     

EC	3.2.1.1	3.2.1.98	3.2.1.-	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	32	371	4.1e-153	0.9970760233918129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11318	AmyAc_bac_fung_AmyA	0.0	5	392	1	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.
PRK09441	PRK09441	0.0	4	479	2	479	cytoplasmic alpha-amylase; Reviewed
cd11314	AmyAc_arch_bac_plant_AmyA	2.57e-46	7	394	1	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.
COG0366	AmyA	2.00e-25	23	372	28	359	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	3.69e-25	33	367	13	324	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
QNM10998.1	0.0	1	491	1	491
QUN13273.1	2.62e-209	5	484	3	477
QWT52923.1	6.14e-207	5	479	4	479
QNL99097.1	2.49e-206	5	479	4	479
ADD61689.1	7.10e-206	5	479	4	479

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UZU_A	9.28e-193	5	480	5	480	Three-dimensionalstructure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
6TOY_A	2.65e-192	5	479	4	481	Crystalstructure of Bacillus paralicheniformis wild-type alpha-amylase [Bacillus licheniformis],6TOZ_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with acarbose [Bacillus licheniformis],6TP0_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with maltose [Bacillus licheniformis],6TP1_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with maltotetraose [Bacillus licheniformis],6TP2_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with beta-cyclodextrin [Bacillus licheniformis]
1OB0_A	7.09e-190	5	479	4	481	Kineticstabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface [Bacillus licheniformis]
1BLI_A	2.87e-189	5	479	4	481	BacillusLicheniformis Alpha-Amylase [Bacillus licheniformis]
1HVX_A	4.33e-189	5	480	5	482	BACILLUSSTEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P06279	5.36e-188	5	480	39	516	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P06278	4.94e-187	5	479	33	510	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P00692	5.31e-182	1	479	26	512	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P19571	1.22e-176	4	479	38	516	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P26612	3.38e-142	5	479	3	490	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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000223_00228.