CAZyme Information: MGYG000004073_00181

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; UBA7001
• CAZyme ID: MGYG000004073_00181
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
486	MGYG000004073_1|CGC1	55794.56	4.8453

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004073	1933457	MAG	United Kingdom	Europe

• Gene Location: Start: 158204; End: 159664 Strand: -

Full Sequence      

MPRNDTMMQYFEWYLPSDSTLWNKLTKEAKHLENIGLTHLWLPPAYKGAGGKEDVGYGVY
DLYDLGEFNQKGDIPTKYGTKDEYINAVKVLRENNIKVLADIVLNHKMGADETEDVLAIQ
DDFSNRNVSLTDALPIRVWTKYTFPGRGDTYSSFKWNWTHFHGIDWDENTGKAAIYKFYG
KHWDENVDKENGNYDYLMGADIDLNNVDVVKELTNWGKWYLDTTSVDGFRLDAVKHIRGE
FYPEWLSELRNYTGKKLFAVGEYWSSNISVINEYIEKTGGCMSLFDVPLHYNFYRASISN
GQFNMSQIFEGTLVKTNPEKAVTFVDNHDTEPGQALQSWILDWFKPLAYSLILLRKDGFP
CVFYGDYYGIPEKQVESKKSMLDILLKVRKYYAYGDQYDYFNSNHIIGFTRLGDYDHPNS
GLAVVMSDQNGGCIQMNVGKKLANTVFYDCTGNLSETVYVDSEGNGIFYCKDGSVSVWIK
QGEAVN

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	31	370	5e-152	0.9970760233918129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11318	AmyAc_bac_fung_AmyA	0.0	4	391	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	2	479	1	479	cytoplasmic alpha-amylase; Reviewed
cd11314	AmyAc_arch_bac_plant_AmyA	2.32e-51	7	368	2	276	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.
PLN02784	PLN02784	1.56e-23	7	390	505	833	alpha-amylase
cd11339	AmyAc_bac_CMD_like_2	3.84e-21	199	366	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADO39270.1	2.47e-211	4	480	2	478
ALU16381.1	1.00e-210	4	480	2	478
ARD64410.1	8.16e-210	4	480	2	478
QCT72471.1	3.30e-209	4	480	2	478
QNL99097.1	1.26e-207	1	479	1	479

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UZU_A	2.23e-209	2	486	3	486	Three-dimensionalstructure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
1HVX_A	1.59e-207	2	486	3	488	BACILLUSSTEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]
6AG0_A	4.72e-206	2	486	30	515	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]
6GXV_A	2.07e-200	4	481	6	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.]
2GJP_A	8.29e-193	1	481	3	485	ChainA, alpha-amylase [Sutcliffiella halmapala],2GJR_A Chain A, alpha-amylase [Sutcliffiella halmapala]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P06279	7.06e-207	2	486	37	522	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P19571	3.10e-188	4	481	39	518	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P06278	1.26e-178	4	481	33	512	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P00692	5.45e-178	4	481	33	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P26612	2.09e-139	3	479	2	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
1.000037	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004073_00181.