dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Paenibacillus_A antibioticophila

Lineage

Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A antibioticophila

CAZyme ID

MGYG000001451_02370

CAZy Family

GH13

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1083		118311.64	4.8978

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001451	5573040	Isolate	not provided	not provided

Gene Location

Start: 2492567; End: 2495818 Strand: -

Enzyme Prediction help

EC	3.2.1.98	3.2.1.1	3.2.1.-	3.2.1.60

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	91	464	3.9e-152	0.9972222222222222
CBM26	688	760	3.9e-20	0.9333333333333333

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	46	531	184	673	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	1.75e-46	53	506	4	344	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.
COG0366	AmyA	4.81e-38	52	463	1	355	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	3.67e-36	54	460	2	252	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.
cd11320	AmyAc_AmyMalt_CGTase_like	1.42e-35	54	505	7	389	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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 help

Hit ID	Query Start	Query End	Hit Start	Hit End
AZK49196.1	44	969	126	962
QQZ60411.1	32	1065	45	1085
ASA20374.1	5	1065	3	1080
QMV43648.1	47	1069	48	1088
CAA37453.1	37	1071	41	1182

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2LAA_A	9.77e-35	874	969	2	102	SolutionStrucuture of the CBM25-1 of beta/alpha-amylase from Paenibacillus polymyxa [Paenibacillus polymyxa]
2LAB_A	2.48e-34	973	1067	3	102	SolutionStrucuture of the CBM25-2 of beta/alpha-amylase from Paenibacillus polymyxa [Paenibacillus polymyxa]
2C3G_A	1.03e-31	685	777	5	97	ChainA, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3H_A Chain A, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_B Chain B, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_C Chain C, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_D Chain D, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_E Chain E, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_F Chain F, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_G Chain G, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_H Chain H, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans]
5A2A_A	2.71e-29	48	594	5	444	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	4.68e-29	48	594	39	478	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	1.27e-156	46	540	183	671	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
A0P8X0	5.41e-71	782	1067	811	1186	Alpha-amylase OS=Niallia circulans OX=1397 GN=igtZ PE=1 SV=1
P21543	1.78e-65	849	1071	421	670	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P06547	2.34e-29	975	1069	462	561	Beta-amylase OS=Niallia circulans OX=1397 PE=3 SV=1
P31747	9.48e-28	27	576	26	497	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 6.6.3) OX=29335 GN=cgt 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
0.000864	0.997177	0.001361	0.000235	0.000174	0.000170

TMHMM Annotations download full data without filtering help

start	end
7	24

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