CAZyme Information: MGYG000000824_00398

Basic Information

• Species: CAG-485 sp900552315
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900552315
• CAZyme ID: MGYG000000824_00398
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
957		105721.8	4.6875

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000824	2120674	MAG	China	Asia

• Gene Location: Start: 17563; End: 20436 Strand: -

Full Sequence      

MKRSLLIGAAALLCGASAMAATSFPSRTDFRDESIYFAMTTRFYDGDISNNTYCWDGVKN
VNDPEWRGDFKGLIEKLDYIKALGFTAVWITPVVENGSGLDYHGYHAMNFQKVDPRYESE
DCKFQDLIDAVHARGMKIILDVVLQHNGNFGEEYLCPMFQKDYTQPLDNINKSMKRHPQS
KLPANYDALIPDAQYQARLTLMKNNDNSGKDPENYWHHVGQSWDWDDYSRVWGQIAGDCV
DLNTENPHVYNYITKCYSKFIEMGVDGFRVDTSGHIARVTFNKAFLPKFKAAGEAAKAKR
GGTPFYMFGEVCARAEEVIYRDQNYNCSPCFYTWAEDKDYAWDEDENSWKGLTFSEVAPS
AYSVHPNTAAVLAQADDYQGHSDAILQKSNNAWLNGNDYHTPDYSKSSGFNVIDFPMHWR
FSSAKKAFNVNSQDNLYNDATWNVVYVDGHDYGPNGWNTKSFGGSEAEWAENYSLMFTFR
GIPCIWQGSECYFQKGVVIDEGPHQALKNTARAYFGGYLTGSVNTTDFAEYTGATGNLAA
TLSHPLAMHLQRLNKIRAAVPCLRKGQYSTDGCSGNIAFKRRYVDASTDSYALIAISGDA
SFSNILNGTYTDVITGDVKNVTNGSLSVSCSGQGNLRIYVLSTAKTLAPGKIGTDGKYLY
ASAPATQTQLPYDGQQEAPDTVTQRDDSPGPGPQPEPDDPKPLVVYKDETCAFFHNTSGW
GGNIYAWCWNDKDNYTGGTWPGTVCEYLGNGYWKWSYGSKEIPEAGTYIIFNAGGSQTAN
LTFQNGAVYAADGTVEQVIPEGEEVNPDPQPDPDPDPDPTPDPTEGYTVYFDNGPTTWAT
VNIHYWGGESASSWPGVKMTLCPGSSSVYYYVVPAGTTGLVFNNGGGSQTGDLTALPNHI
YSINGDQGEHSDTGIGGVGVDATAPIYYNMQGIRVLNPSDGIYIVRRGNVVTKEYVR

Enzyme Prediction     

EC	3.2.1.59

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	67	496	4.1e-131	0.997624703087886

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	6.72e-103	31	560	1	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.
cd11320	AmyAc_AmyMalt_CGTase_like	2.29e-44	29	492	1	350	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.
pfam00128	Alpha-amylase	3.83e-39	68	490	1	325	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.
cd11340	AmyAc_bac_CMD_like_3	3.57e-36	35	502	6	364	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.
cd11352	AmyAc_5	3.99e-33	35	276	2	250	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCJ94880.1	2.03e-226	29	659	247	848
QNT65573.1	1.98e-225	12	901	15	853
AIQ52956.1	3.09e-220	23	659	581	1183
AIW42552.1	8.42e-220	26	659	349	948
APQ62224.1	8.42e-220	26	659	349	948

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4E2O_A	6.25e-26	30	311	7	221	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
5A2B_A	2.37e-24	11	311	22	254	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]
5A2A_A	3.72e-24	30	311	6	220	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
6WNI_A	7.40e-23	31	276	32	255	ChainA, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNI_B Chain B, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNU_A Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus]
3VM7_A	1.27e-21	29	276	26	230	ChainA, Alpha-amylase [Malbranchea cinnamomea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	5.50e-31	28	629	742	1185	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q05884	6.30e-27	68	311	98	347	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P08704	2.21e-26	14	623	24	532	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P14014	2.33e-20	4	276	17	268	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA PE=3 SV=1
P19531	4.06e-20	26	285	35	270	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000579	0.998383	0.000251	0.000298	0.000251	0.000222

TMHMM  Annotations     

start	end
5	24