CAZyme Information: MGYG000002154_02368

Basic Information

• Species: UBA5446 sp900546615
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA5446; UBA5446 sp900546615
• CAZyme ID: MGYG000002154_02368
• CAZy Family: GH13
• CAZyme Description: Maltogenic alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
527	MGYG000002154_41|CGC1	57731.45	4.217

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002154	2646561	MAG	Germany	Europe

• Gene Location: Start: 12212; End: 13795 Strand: +

Full Sequence      

MADPNNDTNGWFHHLGDRGTDNSTFGYRFKELAYLADYSQENAAVAEYMEDALNFWAEKG
ISGIRHDATLHMNPAFVKNAKDAVDSENAPITHFGEFFIGRPDSKYSEYASFPDRTGVTN
LDFEFYNSVNQTFGNFSQSMTDFANMLEYTDDDYTYENQFVTFIDNHDVTRFRYVQSNDK
PFHAAIAALLTCRGTPNIYYGTEQYLSAPDSGAGRIYMGAVSDFESTTATQLIKALSDLR
QENDALAYGTTDILYSSNDVVVYSRQFYSKQVIVAINRQPDQSFTVPALNTTLPNGTYND
VLNGLLYGESATVSSGSLQSFTLGGGEVCVWSYNPDLGTDTPRIGNVISTMGRAGNTVYI
YGTGLGGTPTVKFGDATATVVSASDEMIEAIVPANAAVGENTITVTKGSSVSNGFTYTVL
SGDPNQVIFHVNASTNFGETIHIVGSIPELGSWDTDKCTEAMMCPNYPEWFLHVSVPADT
TFSFKFIKKDANGNVTWESCENRVITSSSSPAGTIDTPVYTWGVNYT

Enzyme Prediction     

EC	3.2.1.116	2.4.1.19

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	2	206	1.1e-67	0.6612903225806451
CBM20	426	510	4.6e-28	0.9333333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11320	AmyAc_AmyMalt_CGTase_like	1.16e-95	1	241	147	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	4.89e-31	426	517	2	95	Starch binding domain.
cd05467	CBM20	1.52e-29	426	522	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	3.45e-26	427	515	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	8.73e-26	36	243	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AMX84409.1	7.21e-250	1	522	237	765
AMX04264.1	7.34e-250	1	522	222	746
AID53183.1	1.18e-249	1	522	236	760
QXJ37788.1	2.36e-248	1	522	237	765
ADV79284.1	1.04e-244	1	522	228	755

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1QHO_A	5.92e-116	8	515	164	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	8.17e-109	6	515	169	681	Crystalstructure of Alpha-CGT from Paenibacillus macerans at 1.7 Angstrom resolution [Paenibacillus macerans]
3BMV_A	1.04e-108	6	515	170	677	ChainA, Cyclomaltodextrin glucanotransferase [Thermoanaerobacterium thermosulfurigenes],3BMW_A Chain A, Cyclomaltodextrin glucanotransferase [Thermoanaerobacterium thermosulfurigenes]
1A47_A	1.04e-108	6	515	170	677	CGTASEFROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR [Thermoanaerobacterium thermosulfurigenes],1CIU_A Thermostable Cgtase From Thermoanaerobacterium Thermosulfurigenes Em1 At Ph 8.0. [Thermoanaerobacterium thermosulfurigenes]
6AIJ_A	1.95e-108	6	515	190	702	Cyclodextringlycosyltransferase from Paenibacillus macerans mutant N603D [Paenibacillus macerans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P19531	7.68e-115	8	515	197	713	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 SV=2
P04830	8.84e-108	6	515	196	708	Cyclomaltodextrin glucanotransferase OS=Paenibacillus macerans OX=44252 GN=cgtM PE=1 SV=2
P26827	1.13e-107	6	515	197	704	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2
P31797	7.47e-105	6	515	196	705	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P30920	2.37e-100	6	515	203	713	Cyclomaltodextrin glucanotransferase OS=Niallia circulans OX=1397 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002154_02368.