dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

HGM12814 sp900770165

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; HGM12814; HGM12814 sp900770165

CAZyme ID

MGYG000003581_00701

CAZy Family

GH13

CAZyme Description

Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
474		53402.15	4.7629

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003581	2356172	MAG	Fiji	Oceania

Gene Location

Start: 5297; End: 6721 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000003581_00701.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	63	328	1.1e-90	0.9849624060150376

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	2.95e-126	54	402	1	352	Alpha amylase catalytic domain found in bacterial 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 Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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.
cd11317	AmyAc_bac_euk_AmyA	9.08e-37	55	325	2	238	Alpha amylase catalytic domain found in bacterial and 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 AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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	4.16e-19	65	265	28	238	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	4.91e-16	53	363	11	255	Alpha amylase catalytic domain family. 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; and 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 this 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.
smart00642	Aamy	9.65e-15	67	146	20	94	Alpha-amylase domain.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDY86356.1	8.22e-116	12	471	9	471
ASR47410.1	1.16e-115	12	471	9	471
QYK62214.1	1.97e-115	25	471	33	479
APB71173.2	1.97e-115	25	471	33	479
AWB44629.1	2.31e-114	46	471	50	475

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UA7_A	3.84e-101	53	471	4	419	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	8.39e-101	53	471	7	422	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
3DC0_A	2.42e-99	53	471	4	419	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1CLV_A	1.24e-21	56	332	12	295	YELLOWMEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR [Tenebrio molitor],1JAE_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE [Tenebrio molitor],1TMQ_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR [Tenebrio molitor]
1VIW_A	2.25e-21	56	332	12	295	TENEBRIOMOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	3.54e-99	30	471	24	463	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	9.25e-89	37	471	39	460	Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2
P30269	1.92e-62	50	471	143	605	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
O76263	1.04e-24	56	331	30	315	Alpha-amylase-related protein OS=Drosophila willistoni OX=7260 GN=Amyrel PE=3 SV=1
Q9GQV3	3.50e-24	56	330	32	316	Alpha-amylase-related protein OS=Drosophila jambulina OX=111875 GN=Amyrel PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.002684	0.996076	0.000327	0.000296	0.000278	0.000289

TMHMM Annotations download full data without filtering help

start	end
7	24

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