CAZyme Information: MGYG000004852_00656

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium
• CAZyme ID: MGYG000004852_00656
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1024		114477.86	4.4684

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004852	2526742	MAG	China	Asia

• Gene Location: Start: 132; End: 3206 Strand: +

Full Sequence      

MKKKNFNRIIVGALIFTIISSSLVTGATIKVTTFNNSYLNRSQENENVLKVDVNEYGQVT
YCTTSNIDESINSQEERKFSWDNATVYFALTDRFSNGDTSNDHSYGRGLDQNGNVQEGYE
NNPGGFHGGDLKGLTEKIKEGYFKDLGVNAIWITAPYEQIHGFTSGNAAGGNGQDNGEGF
PYYSYHGYWTLDYSNIDANMGTEEDFRNFVDTAHSQGIRVVMDIVLNHVGYTTMKDADEY
GFGSMKSGWEDYYYGNLRDLDGGAVEANTWYNKEDSTWATNWWGDDFVRVSAGYAGYEKH
SDGGGYTNPLSGLPDIKTESKEEVDLPAILETKWKREGRYEEEMAELNEFFTKRNLPRTP
RNYVIKWLTDYIRDFGVDGFRCDTVNHVEMEGWAALNEEADIAFEEYKANNPDKVLDQDA
DFWTTGESWGHGVTKSAFFTSGGFNSIINFSFKGASTSNIKAKYNSLKAVNKDDNFNVLS
YISSHDDLLHDRNSLIDGGTSLLLAPGAVQIFYGDETARPVGWKDFFTRGEYKDQMYRTS
MNWDDLENPNSQASKTLSHWQKLGQFRNNHLSVGAGEHIDIADSPYTFGRIYNKDGNSDK
VVCVIGATGTIDVDVSKVFNDGSKVRDAYTGVITTVQNGKATFTAGENGVILIEKGDKSP
DVGISVQGCEYYEDTLELALYVTNSKVGKYSIDGGEEKTFTNGEKIIIGEGLAYDTTTTV
TVSAKNLEGESSLTYTYTKMDPLKKRVKVHYYNSEGWSNPYVYMYDESDGESKEVAAWPG
VKMEDEGNGWYSYNQVGWLNSQVIFSNAGASQNPGQNQPGFQVNGEMWYKDGIWYKSNPD
GPTISSISFDKNSPQFINEDIKIIANATGKGELQYKFEVNKEGTSTFISDYTTNNSVTWV
PTEIGSYTVIVTVKDESGKEVTSTKTYLIEKINLVINSVTTSEVEGKVGEPITITTDALG
SGTLQYKVSVHEIKEGWRALTSKYTSEKEIDWTPEEDGVYKIWVDVKDEDGNKEYKCISI
NIKK

Enzyme Prediction     

EC	3.2.1.98	3.2.1.1	3.2.1.-	3.2.1.60

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	129	517	2.2e-139	0.9972222222222222
CBM26	748	823	2.7e-20	0.96

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	2.37e-177	69	604	175	678	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	6.26e-46	85	570	4	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.
cd11338	AmyAc_CMD	2.02e-42	92	570	10	381	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.
cd11320	AmyAc_AmyMalt_CGTase_like	1.01e-35	85	283	6	168	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.
COG0366	AmyA	1.13e-34	84	605	1	481	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGF57034.1	0.0	1	850	1	844
ANF15233.1	0.0	76	834	37	795
QCJ03813.1	0.0	76	834	37	795
ALS18108.1	0.0	76	834	37	795
QCJ05919.1	0.0	76	834	37	795

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	7.17e-25	80	640	5	433	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	8.32e-25	73	640	34	467	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]
4E2O_A	9.60e-25	75	518	1	330	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
3WMS_A	3.35e-20	66	242	28	182	Thecrystal structure of Y195I mutant alpha-cyclodextrin glycosyltransferase from Paenibacillus macerans [Paenibacillus macerans]
1CYG_A	1.22e-19	78	707	6	544	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	1.54e-113	69	595	174	666	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	4.55e-20	118	455	86	375	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P16950	6.99e-19	84	653	386	919	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P31797	7.09e-19	78	707	37	575	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P27036	1.22e-18	78	228	34	162	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
0.002783	0.995622	0.000843	0.000304	0.000217	0.000203

TMHMM  Annotations     

start	end
7	29