CAZyme Information: MGYG000000707_00305

Basic Information

• Species: Prevotella sp900546575
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900546575
• CAZyme ID: MGYG000000707_00305
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1047	MGYG000000707_4|CGC2	116651.4	4.6581

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000707	3151200	MAG	Kazakhstan	Asia

• Gene Location: Start: 78587; End: 81730 Strand: +

Full Sequence      

MWALLLLMLIALPVMADDFNSQRTDFRDESIYFMITTRFYDGDPKNNVLCWDNKQCQIDT
GDPCWRGDFQGVIDKLDYIKALGFTAIWITPVVQNASGYDYHGYHAMDFTHVDCRYQSGD
GSKSGDVMFQELIDKAHAKGIKIILDIVLNHTGNFGEENLCKEFERNTKLRNQAEIDACM
IPNSDVLGSDYLTILGKDQYQRRLALMKNTDGNNHDSHNYWHHVATQWNWDEPNRWWGQI
AGDCVDLNTENDAVAEYLVKCYGEFIKMGVDGFRIDTSGHISRLTFNKVFIPQFQALGEQ
YKSKRLNQAPFFMYGEVCARFGSVQYRGQDCLSPYFYTWKSDQEIMNSWNSDATWWDKQV
VPEGADPLGNMTLCLKDVADSPTSNNTFMLNGAWHKPDYTQSSGFNVIDFPLHYNFSNAG
SAFRLAKDGDAKYNDATYNVVYVDSHDYGPQPNDRVRFGGDNAQWAENLSLMFTFRGIPC
IYYGSEVGFRRGQVIDDGPNGPLFNTGRAYFGGYITGDVEATDFGKYTASGNVNATLNHD
LAQHLIRLNKIRQAVLALRKGQWTDEGCTSTSGIAFKRAYENSYALVALNGGATFTDCPE
GTYTDIVTGKTYTGSTITVDAPETQGQVRVLVKDWTGGVVGEDGPFIYTSSAKSKDGQAY
DGQEEAGTDIYYGSEDIEQDAAVVFNPNGGNFRTETVTVTATLNNGAKSGWYQIEGEDKV
ELSSEGSTFTIGADMKFGDTKKVKWGATNDDGTEYSGTTTYRKVDPNASIIVYVKADKAP
NLYAWTKGGEKTNELNGAWPGNRLTTTQTIEGVDYYMFVADGVESFNMILNNGGTSQTSN
ITNITATTFFSYDGGSGYEVLSDIPVPEPNPNPNPNPEPEPDPTPVPNPTGKFYVYFAAP
TSWNNVKAWVWDSNIKDKQKNNYTGGNWPGEDCVKTSKKYNGMSIWMWEYKGDKTDMPTH
IIFNNGGSEQTADLEYQNGKCYDFNGVNSSINITTAINGINANAAKKMIKVYTLNGECVG
VMSNLNSATYTLRPGIYIANGRKFVVR

Enzyme Prediction     

EC	3.2.1.59

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	66	492	1.8e-123	0.997624703087886

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	1.47e-110	27	555	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.
pfam00128	Alpha-amylase	2.27e-46	67	489	1	328	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	5.84e-44	31	500	6	366	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	1.78e-42	25	486	1	348	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.
cd11352	AmyAc_5	1.40e-34	31	489	2	397	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
QNT65572.1	0.0	1	1047	8	1117
QNT65573.1	0.0	1	1047	8	1114
QNT65571.1	0.0	6	1047	1	1114
QCT07981.1	1.99e-190	18	644	130	742
QCT07168.1	1.56e-187	17	644	134	790

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WMS_A	1.24e-24	6	619	12	503	Thecrystal structure of Y195I mutant alpha-cyclodextrin glycosyltransferase from Paenibacillus macerans [Paenibacillus macerans]
1I75_A	1.46e-24	21	621	7	473	CRYSTALSTRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN [Bacillus sp. (in: Bacteria)],1I75_B CRYSTAL STRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN [Bacillus sp. (in: Bacteria)],1PAM_A CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1PAM_B CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1UKQ_A Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose [Bacillus sp. 1011],1UKQ_B Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose [Bacillus sp. 1011]
5A2A_A	1.78e-24	20	153	1	119	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
1V3K_A	1.93e-24	21	621	7	473	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3K_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3M_A Chain A, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3M_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]
1V3J_A	1.93e-24	21	621	7	473	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3J_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3L_A Chain A, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3L_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	2.94e-36	20	590	738	1144	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P09121	4.05e-25	1	621	13	500	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 38-2) OX=1412 GN=cgt PE=1 SV=2
P14014	1.66e-24	16	609	36	496	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA PE=3 SV=1
P31746	1.94e-23	8	621	19	494	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1-1) OX=29334 GN=cgt PE=1 SV=1
P26827	1.98e-23	1	609	12	489	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA 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
0.000219	0.999158	0.000147	0.000162	0.000139	0.000141

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000707_00305.