CAZyme Information: MGYG000000861_00171

Basic Information

• Species: Olsenella_B sp900548775
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Atopobiaceae; Olsenella_B; Olsenella_B sp900548775
• CAZyme ID: MGYG000000861_00171
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
499		55645.58	4.6172

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000861	2145101	MAG	China	Asia

• Gene Location: Start: 61123; End: 62622 Strand: +

Full Sequence      

MVINTKNGLMLQAFSWYLPADGQHWRRLAKMAPRFAEEGFTSVWMPPAYKGQAGAEDVGY
GVYDLWDLGEFDQKGSVRTKYGTCHEYLAAIRAIQEQGVNVLADVVLNHRMGADGTQLVL
AQECDAQDRTKPVGDPREIRAYTRFEFPGRAGKLDRYQWGITDFTGVDYDELEGTTGVYR
FVGKEWSHEVSDELGNYDYLMGADVDLDDPSVRAQLATWGAWYLGLTGVDGVRLDAVKHM
SRSFYLDWLARMREKTGKELFAVGEYWSQNVDELRGYLGREGAMSLFDVPLHFNFYRAST
AGDNIDLTHILDGSLVSVDPIHAVTFVDNHDTQPDQALESTVEPWFKPLAYALILLREAG
YPCVFMGDLFGLPNDQIPAVPELELLMEVRRRFAYGEQRDWFDEKDLVGWTREGTARHGV
SGAAVLLSTRSGNATKRMCVGAGHAGETWRCVLGVDGTVTIDGEGWAEFSTGGARLTVYL
PAATADKLDSIPILVRPEA

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	35	371	3.7e-142	0.9912280701754386

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09441	PRK09441	0.0	5	479	1	478	cytoplasmic alpha-amylase; Reviewed
cd11318	AmyAc_bac_fung_AmyA	0.0	7	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.
cd11314	AmyAc_arch_bac_plant_AmyA	2.99e-46	10	394	2	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	3.50e-21	202	368	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.
PLN02784	PLN02784	4.00e-19	5	392	498	834	alpha-amylase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SDR65167.1	3.51e-217	7	489	3	486
QUC02472.1	4.84e-205	7	490	2	486
ALC98635.1	3.81e-203	7	496	13	503
AMD98267.1	9.88e-200	4	490	15	501
QHO91531.1	6.74e-199	6	489	13	495

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UZU_A	4.36e-173	7	497	5	496	Three-dimensionalstructure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
6TOY_A	4.46e-173	5	480	2	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	4.46e-173	7	480	4	481	Kineticstabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface [Bacillus licheniformis]
1BLI_A	6.32e-173	7	480	4	481	BacillusLicheniformis Alpha-Amylase [Bacillus licheniformis]
1VJS_A	1.80e-172	7	480	4	481	StructureOf Alpha-Amylase Precursor [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P06278	9.30e-172	7	480	33	510	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P06279	2.10e-169	7	497	39	532	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P19571	1.28e-165	4	480	36	516	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P00692	1.16e-157	4	480	30	512	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P26612	2.40e-136	6	480	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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000861_00171.