dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Clostridium_E merdae

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Clostridium_E; Clostridium_E merdae

CAZyme ID

MGYG000002420_00078

CAZy Family

GH13

CAZyme Description

Amylopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
614		69871.53	4.7576

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002420	2748860	Isolate	not provided	not provided

Gene Location

Start: 74606; End: 76450 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000002420_00078.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	179	508	1.1e-132	0.9936708860759493

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	126	541	1	384	Alpha amylase catalytic domain found in 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). 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.
PRK10785	PRK10785	1.57e-117	120	584	115	568	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	4.25e-88	3	541	6	572	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
pfam00128	Alpha-amylase	5.84e-59	179	508	1	334	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
cd11353	AmyAc_euk_bac_CMD_like	1.03e-57	128	541	3	361	Alpha amylase catalytic domain found in eukaryotic and 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 mainly 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
CAB1239245.1	1.52e-303	1	614	1	614
QAT48387.1	6.78e-289	1	614	1	615
QNK39367.1	5.99e-283	1	612	1	613
QEY35300.1	5.08e-278	1	606	1	608
BCI61467.1	2.96e-273	2	605	6	609

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1SMA_A	8.60e-78	118	609	126	580	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
1EA9_C	1.07e-77	64	612	66	578	Cyclomaltodextrinase[Bacillus sp. (in: Bacteria)],1EA9_D Cyclomaltodextrinase [Bacillus sp. (in: Bacteria)]
5BN7_A	8.65e-77	121	605	119	597	Crystalstructure of maltodextrin glucosidase from E.coli at 3.7 A resolution [Escherichia coli K-12]
1GVI_A	1.25e-76	118	609	126	580	Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.]
2Z1K_A	4.29e-76	123	610	3	470	CrystalStructure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_B Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_C Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_D Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P16950	5.48e-108	3	553	256	839	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P36905	1.86e-107	3	584	259	881	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38939	5.39e-107	3	553	256	838	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P38536	1.96e-101	3	584	259	880	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
Q08341	1.62e-80	121	612	128	582	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 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
1.000060	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002420_00078.

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