CAZyme Information: MGYG000000073_00040

Basic Information

• Species: GCA-900066905 sp900066905
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; GCA-900066905; GCA-900066905; GCA-900066905 sp900066905
• CAZyme ID: MGYG000000073_00040
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
489	MGYG000000073_1|CGC1	54398.82	5.1942

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000073	2615710	Isolate	United Kingdom	Europe

• Gene Location: Start: 53149; End: 54618 Strand: -

Full Sequence      

MNQTLIQYFEWYLPSDGAHWRRTAGDAQHLAQLGFTGVWLPPAYKGAKGGADTGYAVYDL
YDLGEFDQKGSVPTKYGTRDEYLAAIAALHQAGLAVYPDIVLNHRIGADETERVTVRRSD
EADRTREIGGEEQIDAWTRFTFPGRGGKYSTFQWNWTHFNAVDWDNGGQRSAIFRFEGKP
WERDVDKERGNFDYLMGANLDTKNPQVVDELDAFGQWYLQTTGADGFRLDAVKHIRFDFF
THWLERLRSLNGRPLFAVGEYWNGEVGMLTHYLDACGRVMQLFDVPLHYNFYRASTSGGN
FDMRRIFEGTLTAARPARAVTFVDNHDTQCGQALHSPVQSWFKPLCYALILLREAGLPCV
FYGDYYGTGDGTQPPLQGVLDVLLRARKYCAYGEQTDYFDDYNIVGWTRAGDAAHPGSGL
AAVLSDGPGGEKEMCMGVAFAGRRFYDALGGCPGRVVIGENGCARFPVGGGAVALWLPED
GALGLMGGQ

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	29	368	6.9e-151	0.9970760233918129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11318	AmyAc_bac_fung_AmyA	0.0	2	389	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	476	3	478	cytoplasmic alpha-amylase; Reviewed
cd11314	AmyAc_arch_bac_plant_AmyA	1.08e-48	5	388	2	292	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	2.02e-25	29	415	37	378	Glycosidase [Carbohydrate transport and metabolism].
smart00642	Aamy	5.58e-23	3	105	1	95	Alpha-amylase domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALU16381.1	2.13e-208	1	477	1	477
ADO39270.1	2.13e-208	1	477	1	477
ARD64410.1	2.46e-207	1	476	1	476
QCT72471.1	1.41e-206	1	477	1	477
ARD65935.1	7.67e-204	2	479	3	479

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UZU_A	1.39e-196	2	479	5	481	Three-dimensionalstructure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
1HVX_A	2.44e-195	2	479	5	483	BACILLUSSTEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]
6AG0_A	2.34e-192	2	479	32	510	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]
1W9X_A	1.07e-190	2	477	2	479	ChainA, Alpha Amylase [Sutcliffiella halmapala]
2GJP_A	1.23e-190	2	477	6	483	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	4.32e-194	2	479	39	517	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P06278	1.86e-186	1	477	32	510	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P19571	1.85e-185	2	477	39	516	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P00692	2.29e-180	1	479	32	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P26612	5.78e-148	2	480	3	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
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000073_00040.