dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

UBA5446 sp900545405

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA5446; UBA5446 sp900545405

CAZyme ID

MGYG000004557_01792

CAZy Family

GH13

CAZyme Description

Maltogenic alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
572	MGYG000004557_49\|CGC1	62653.51	4.1606

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004557	2548917	MAG	France	Europe

Gene Location

Start: 13088; End: 14806 Strand: +

Enzyme Prediction help

EC	3.2.1.116	2.4.1.19

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	43	251	1.4e-68	0.6741935483870968
CBM20	471	555	5.2e-28	0.9333333333333333

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11320	AmyAc_AmyMalt_CGTase_like	4.12e-96	33	286	131	388	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.
pfam00686	CBM_20	5.40e-31	471	562	2	95	Starch binding domain.
cd05467	CBM20	1.54e-29	471	567	1	96	The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
cd05808	CBM20_alpha_amylase	3.77e-26	472	560	3	90	Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
cd11339	AmyAc_bac_CMD_like_2	1.79e-25	81	288	125	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AMX04264.1	2.08e-271	5	567	181	746
AID53183.1	3.39e-271	5	567	195	760
AMX84409.1	5.54e-269	11	567	202	765
QXJ37788.1	1.82e-267	11	567	202	765
ADV79284.1	2.27e-263	11	567	193	755

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1QHO_A	7.98e-117	36	560	150	680	FIVE-DOMAINALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX [Geobacillus stearothermophilus],1QHP_A Five-Domain Alpha-Amylase From Bacillus Stearothermophilus, Maltose Complex [Geobacillus stearothermophilus]
4JCL_A	3.56e-111	33	560	143	681	Crystalstructure of Alpha-CGT from Paenibacillus macerans at 1.7 Angstrom resolution [Paenibacillus macerans]
6AIJ_A	8.58e-111	33	560	164	702	Cyclodextringlycosyltransferase from Paenibacillus macerans mutant N603D [Paenibacillus macerans]
6L2H_A	9.90e-111	33	560	143	681	CGTasemutant-Y167H [Paenibacillus macerans]
3WMS_A	1.35e-110	33	560	174	712	Thecrystal structure of Y195I mutant alpha-cyclodextrin glycosyltransferase from Paenibacillus macerans [Paenibacillus macerans]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P19531	1.04e-115	36	560	183	713	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 SV=2
P04830	3.89e-110	33	560	170	708	Cyclomaltodextrin glucanotransferase OS=Paenibacillus macerans OX=44252 GN=cgtM PE=1 SV=2
P26827	1.49e-108	45	560	191	704	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2
P31797	1.93e-105	45	560	190	705	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P30920	1.11e-101	45	560	197	713	Cyclomaltodextrin glucanotransferase OS=Niallia circulans OX=1397 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999994	0.000053	0.000002	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000004557_01792.

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