CAZyme Information: MGYG000001723_02090

Basic Information

• Species: UBA5446 sp004553625
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA5446; UBA5446 sp004553625
• CAZyme ID: MGYG000001723_02090
• CAZy Family: GH13
• CAZyme Description: Maltogenic alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
756	MGYG000001723_85|CGC1	83243.81	4.2854

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001723	2328137	MAG	Sweden	Europe

• Gene Location: Start: 3469; End: 5739 Strand: +

Full Sequence      

MKGKLPERRTMKEKKRILSLLLSLLLITALLLTPAGAQGFNTELLSVTQSTITDDYLGPV
TPKDVIYQIITDRFYDGDPTNNIPAGFDPDLFDGTGTDIRLYQGGDWQGIIDQIPYLKSM
GITAVWISAPYANRDQATHDGWTSYHGYHARNYFTTNKHFGTMAEFDELQQELTDAGIKL
VIDFVTNHSSDSRYDGKIYEPDRNSAGEFVFDSAGEPVDYNNDGTTENLVADPNNDTNGW
FHHLGDRGTDNSTFGYRFKELAYLADYSQENAAVAEYMEDALNFWAGKGISGIRHDATLH
MNPAFVKNAKDAVDSENAPITHFGEFFIGRPDSKYSEYASFQDRTGVTNLDFEFYNSVNQ
TFGNFSQSMADFANMLEYTDDDYTYENQFVTFIDNHDVTRFRYVQSNDKPFHAAIAALLT
CRGTPNIYYGTEQYLSAPDSGAGRIYMGAVSDFESTTATQLIKALSDLRQENDALAYGTT
DILYSSNDVVVYSRQFYSKQVIVAINRQPDQSFTVPALNTTLPNGTYNDVLNGLLYGESA
TVSSGSLQSFTLGGGEVCVWSYNPDLGTDTPRIGNVISTMGRAGNTVYIYGTGLGGTPTV
KFGDATATVVSASDEMIEAIVPANAAVGENTITVTKGSSVSNGFTYTVLSGDPNQVIFHV
NASTNFGETIHIVGSIPELGSWDTDKCTEAMMCPNYPEWFLHVSVPADTTFSFKFIKKDA
NGNVTWESCENRVITSSSSPAGTIDTPVYTWGVNYT

Enzyme Prediction     

EC	3.2.1.116	2.4.1.19

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	104	435	3.5e-107	0.9967741935483871
CBM20	655	739	7.8e-28	0.9333333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11320	AmyAc_AmyMalt_CGTase_like	1.28e-168	60	470	1	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.
cd11339	AmyAc_bac_CMD_like_2	2.00e-62	63	472	2	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.
cd11340	AmyAc_bac_CMD_like_3	1.27e-50	61	441	1	361	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.
pfam00128	Alpha-amylase	6.48e-49	105	436	1	329	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.
cd11319	AmyAc_euk_AmyA	6.59e-48	65	470	10	370	Alpha amylase catalytic domain found in 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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
AMX84409.1	0.0	26	751	13	765
ADV79284.1	0.0	14	751	6	755
ABY94335.1	0.0	14	751	6	755
QXJ37788.1	0.0	26	751	13	765
AID53183.1	0.0	11	751	1	760

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1QHO_A	9.03e-152	64	744	9	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	3.08e-146	64	744	15	681	Crystalstructure of Alpha-CGT from Paenibacillus macerans at 1.7 Angstrom resolution [Paenibacillus macerans]
6AIJ_A	8.07e-146	64	744	36	702	Cyclodextringlycosyltransferase from Paenibacillus macerans mutant N603D [Paenibacillus macerans]
6L2H_A	8.62e-146	64	744	15	681	CGTasemutant-Y167H [Paenibacillus macerans]
3WMS_A	1.36e-145	64	744	46	712	Thecrystal structure of Y195I mutant alpha-cyclodextrin glycosyltransferase from Paenibacillus macerans [Paenibacillus macerans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P19531	2.15e-152	14	744	2	713	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 SV=2
P04830	3.74e-145	64	744	42	708	Cyclomaltodextrin glucanotransferase OS=Paenibacillus macerans OX=44252 GN=cgtM PE=1 SV=2
P26827	1.03e-143	64	744	42	704	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2
P31797	9.39e-138	63	744	42	705	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P27036	2.57e-135	25	751	15	703	Cyclomaltodextrin glucanotransferase OS=Bacillus ohbensis OX=1481 GN=cgt PE=3 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
0.000896	0.998124	0.000306	0.000257	0.000212	0.000193

TMHMM  Annotations     

start	end
17	39