CAZyme Information: MGYG000001082_01527

Basic Information

• Species: Ruminococcus_E sp900755995
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp900755995
• CAZyme ID: MGYG000001082_01527
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
797		89383.57	4.2832

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001082	2310000	MAG	Sweden	Europe

• Gene Location: Start: 30643; End: 33036 Strand: +

Full Sequence      

MIKIKKWCALVLSVMLVIAMGLVTANAADQTAEEVAADAETGITVHYQNEGLAQPYIYLW
NSLPTNSAMSDSYPGEKMTNSGNGWFTYYISNVTAVNMIFTDKDGNQYSRELRRTTGEWW
YRNNRWTNHNPDDVDPVSSVDMREESIYFVMTTRFYDGDSGNNVHCWDDSQANNPDSDPA
WRGDFKGLADKLDYIKALGFSAIWVTPVVTNGSGYDYHGYHAMDLATPDARYESTDFTFQ
DLIDAVHSKGMKIIQDVVFQHTGNFGESYFCNLFERDLTKDLSNLEESMIPTDLLLSTFG
LNSPEEYWAQKPAIQYQQRLNIMKNLEYTGEGGNSTGNLPAAKDYDINKLSQSDKYNVDN
YYHSGYFQSLNWDDWTCKFAQIAGDCVDLNTENPAVAEHIVDVYSDYISMGVDGFRVDTV
RHVPRLALNLMYNDQLYDAAKASGNNHFLMFGEICTRYTQIWYRGHAEESSPYYTWKESN
PKWADLWSWGSSVEDINNNMNVVFDHYLEEDDTTDEPTSDNAYLDGITYHTPDRSMASGM
EAIDFQMHRMFGNASNAYNFAKSTDQYYNDATYNVMYVDSHDYAPEQPDEKNRFAGGTQT
WAENLDLMFTFRGIPCVYYGSEVEFMKGAVIDVGPNAPLSTTGRAYFGDYLEGDVTATDF
SEFTASGTVADTLASPLSQHLSKLNAIRRAIPALQKGQYTASSTYVTDGDMSYIRRYTSA
EDGIDSLALVTVSSGATFKNIPNGKYIDAVTGDVKNVTNGTLTVSSIGKANMRVYVCCAD
GFTGIEGEIGGTSSFLK

Enzyme Prediction     

EC	3.2.1.1	3.2.1.98

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	182	628	1.4e-134	0.997624703087886

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	9.57e-114	143	691	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	1.34e-38	141	622	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	1.24e-31	183	623	1	326	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	6.20e-30	147	721	3	475	Glycosidase [Carbohydrate transport and metabolism].
cd11340	AmyAc_bac_CMD_like_3	1.40e-29	138	628	1	357	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
QCT07168.1	0.0	1	797	1	795
QCT07981.1	1.67e-267	1	797	1	747
QEH70845.1	1.33e-255	43	797	250	963
BCJ94880.1	2.03e-239	34	797	125	849
AET61000.1	2.97e-225	90	797	320	948

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	1.20e-16	143	263	7	119	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	1.50e-16	143	263	41	153	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]
6SAU_A	5.16e-16	183	264	58	137	ChainA, alpha amylase [Cordyceps farinosa],6SAU_B Chain B, alpha amylase [Cordyceps farinosa]
7P4W_A	9.85e-16	137	266	1	127	ChainA, Alpha-amylase [Aspergillus oryzae]
2GUY_A	9.94e-16	137	266	1	127	Orthorhombiccrystal structure (space group P21212) of Aspergillus niger alpha-amylase at 1.6 A resolution [Aspergillus oryzae],2GVY_A Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 A resolution [Aspergillus oryzae],2GVY_B Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 A resolution [Aspergillus oryzae],3KWX_A Chemically modified Taka alpha-amylase [Aspergillus oryzae],3VX0_A Crystal Structure of alpha-amylase from Aspergillus oryzae [Aspergillus oryzae RIB40],3VX1_A Crystal Structure of alpha-Amylase from Aspergillus oryzae [Aspergillus oryzae RIB40],6TAA_A Structure And Molecular Model Refinement Of Aspergillus Oryzae (Taka) Alpha-Amylase: An Application Of The Simulated-Annealing Method [Aspergillus oryzae],7TAA_A Family 13 Alpha Amylase In Complex With Acarbose [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	7.37e-28	135	765	736	1185	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q05884	4.48e-25	183	741	98	583	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P08704	1.01e-19	140	765	38	538	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P19531	4.24e-15	129	422	26	265	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 SV=2
O14154	4.74e-15	134	264	20	147	Alpha-amylase mde5 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mde5 PE=2 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
0.000260	0.999064	0.000188	0.000168	0.000151	0.000141

TMHMM  Annotations     

start	end
7	29