CAZyme Information: MGYG000002157_01437

Basic Information

• Species: Amulumruptor sp001689515
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor sp001689515
• CAZyme ID: MGYG000002157_01437
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
880		98720.89	5.072

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002157	2499032	MAG	Germany	Europe

• Gene Location: Start: 8669; End: 11311 Strand: -

Full Sequence      

MKTIKSLVVALVMTCIHMSAFASDFVGTRDDFRDESIYFLLTTRFYDGDPSNNMQCWENQ
EANKGCPPWRGDFKGLIEKLDYIKALGFTAIWMTPIVENASGYDYHGYHAIDMSKVDFRL
ESKDATFENLINEAHSRGIKIILDIVLNHTGNFGEANLFPLFKRDYTKTQSSWIESLIPL
REKDGGKLPNNYYKLDGEAQYQQRIKVMKNGDGKNHDPENIYHHTATNWNWDEPSRWWGQ
IAGDCVDLNTENPKVYNYLVDCYGKFIKMGVDGFRIDTSGHLSPLTMQKVFIPRFEAIAE
ESKAKRGGGPFFMFGEVCARFNDVTYRNRNVLSPWFYQWKITEDYGWDHDPASWEGLVVP
PGKEADHVNIRSCNAFGAANFHDNNQPNSRNILLDGNKYHAVDRSLYSGMSVIDYPMHMY
FRNAKNAFDVRHGDHLYNDASYNVCYTDSHDYGPADSGSRPWKSNEEFAEMMNLLFTWRG
IPCVYYGSETRFRWGHHIDPGPQGGPLDDSGRGYYGGRIKGSVKATDFSSYTDATGNMAV
SLDAPMAHHYRRLNKLRAAIPALRRGQYSTEGCKSDMIAFKRRYTDATIDSYVLVAIGAG
ASFTGIENGHYVDAITGQEANVTDGTLTVESIKTGNMRIYVLDTSLTKAPGKVGTDGPFL
YTATPGGNPELMDPEYDGTEEEPSSNEGPLPDPNFVVNDDWVEPEPPVIEPGDENYTVYF
DNSGSGWASVKTWIWNHLNTSENYTGGSWPGTVMTEDDASGYWKYAFKCENPEAKLMVIF
NNGQGAQTGDFELVNNGIYNASGYTGVNISSTATVYDDGKDEIRIETGADHSLTIISPTE
RKIDIVSPDGCISTVHVTTGRNTISLPRGFYIVGGHKVML

Enzyme Prediction     

EC	3.2.1.59

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	70	495	4.6e-122	0.997624703087886
CBM26	717	791	5.3e-16	0.9333333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	3.56e-100	33	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	1.18e-45	31	489	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.
pfam00128	Alpha-amylase	1.16e-40	71	489	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.
COG0366	AmyA	2.82e-38	37	589	3	477	Glycosidase [Carbohydrate transport and metabolism].
cd11340	AmyAc_bac_CMD_like_3	6.61e-37	37	489	6	352	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
QNT65573.1	7.74e-211	2	799	3	853
QNT65572.1	1.96e-205	1	799	1	854
BCJ94880.1	5.52e-205	31	660	247	848
QNT65571.1	1.41e-204	16	799	5	850
QEH70845.1	1.23e-200	29	660	358	962

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6WNI_A	1.58e-27	33	625	32	499	ChainA, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNI_B Chain B, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNU_A Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus]
4E2O_A	3.91e-27	33	588	8	393	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
5A2A_A	1.76e-25	28	317	2	220	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	2.73e-25	28	317	36	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]
6CGT_A	1.71e-23	26	660	6	507	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	4.73e-29	20	282	725	946	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P08704	5.78e-26	18	629	26	537	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
Q05884	5.69e-25	71	625	98	593	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P30921	1.90e-23	26	666	33	539	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 17-1) OX=72572 GN=cgt PE=1 SV=1
P30920	1.02e-22	26	660	40	541	Cyclomaltodextrin glucanotransferase OS=Niallia circulans OX=1397 PE=1 SV=1

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
0.000259	0.999047	0.000188	0.000165	0.000149	0.000145

TMHMM  Annotations     

start	end
7	26