CAZyme Information: MGYG000004334_00795

Basic Information

• Species: Ruminococcus_E sp002493635
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp002493635
• CAZyme ID: MGYG000004334_00795
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1147	MGYG000004334_9|CGC3	123578.69	4.4045

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004334	2103818	MAG	Israel	Asia

• Gene Location: Start: 68518; End: 71961 Strand: -

Full Sequence      

MKTKKTVKLLSVFVALSLVICCVSFAFANVGAATVKEDTAVSAIAGSVVEKDGFTWDNAT
VYFLLTDRFKNGNTSNDHSYGRTLDKDGKPISGWDTAPGTFHGGDFAGITQAIEEGYFND
LGVNALWISAPYEQTHGYCDSGAGHFAHYSYHGYYVLDYTETDANFGTPEEFETLVDTAH
EHGLRVIMDIVMNHCGYNTVADMEEFGFGTLLDGATDFKYVIENVSDFNKHIDYQTSAED
WGKWWGPDWIRSGLPGYTEGGGSNELMSLAGLPDFKTEQTTPVSIPEVLKTKWTKEGTYN
EKIAKYGSSNTVTGYLTSWLAEWVRKYGVDGFRCDTAKHVEKSSWKQLKTACVDALAEWR
QNNPDKPGADWQQDFWMTGEAWDKGVGYDEYYTQGGFDSMINFETWGAGVLASSRVAGLY
QGYADAINTKEDFNVLSFISSHDALLTRGDTNTMIYTGSAFLLTPGGVQIYYGDESNRPM
FDGLAFDGAGGSGHSLRSDMNWDSLDQTVLAHWQKVGQFRKDHVAIGAGSNIKLSATNGV
AFARTYDKNGVSDKAAAVIGASSNADITIDVSSIWSDGQLLMNAYDQSSAIVTDGKVTFN
SGENGTILIQMPDGKPIMSVTGEAKFKGTQTVTVSLEECDSATCSIDGGNKFLVTNGSTF
EIGKTAYEGDTIKITLEATNEKGSSRAVASFYKMFESEEQPTTGDPSTTVPAQKAKIFVK
SDSAPYVYAWAGENTALCGSWPGTQITEKNSEGYYVMDLNTTDTYNVVLSNGSNSNQSKN
FKNLNGETYFEIPSGNYSAAKIGTSGSGDDPSEKSVTFTIKPYSASASYHLYVWAADGSE
LTGGWPGMKLTEKDADGNYIFTVSGYDKVSAIVGTGNDSKRTQDITGIIDGSCIEITNED
CTTYKLTKPEIVLSKFQTLKKEARGVLAMTASDYTVSSWNNVQSVMTSANALIAQGEGVA
DEALVVSTLEELQNAKAALVLANAGLSYAVKGKSTIKGVAVQGADITVTVDGKTYKTTSD
EITGEFTVEATALTSSSVIKVDVKRNGLSSESYSYNMSNGDITGYVPPTNPTTPTTPTTP
GFVLGDVTGDGKVSVDDATYIQKYIADLVSMTSQQQQAANVDGDNEISIKDATEIQKHVS
GMSSVLG

Enzyme Prediction     

EC	3.2.1.98	3.2.1.1	3.2.1.60	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	104	476	5.8e-141	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	50	551	181	675	alpha-amylase; Reviewed
COG0366	AmyA	1.21e-46	59	551	1	477	Glycosidase [Carbohydrate transport and metabolism].
cd11339	AmyAc_bac_CMD_like_2	3.33e-45	60	523	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	2.71e-44	67	530	10	388	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.
cd00551	AmyAc_family	8.83e-41	60	472	1	253	Alpha amylase catalytic domain 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; and 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 this 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
BCN30960.1	0.0	52	1056	56	1055
QCT06045.1	4.54e-317	32	852	37	853
QCT06087.1	7.14e-206	38	679	35	734
CDM67955.1	4.58e-194	50	773	64	797
CDM67952.1	1.09e-182	50	777	70	808

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	4.72e-31	55	570	5	409	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	6.35e-31	46	570	33	443	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	1.35e-27	50	541	1	383	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1A47_A	1.18e-23	38	634	3	517	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]
6SAO_A	4.23e-23	56	600	6	426	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	4.34e-125	54	551	184	668	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	5.55e-25	92	550	85	553	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P26827	5.31e-23	4	634	2	544	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2
P05618	8.54e-22	47	678	32	582	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1011) OX=1410 GN=cgt PE=1 SV=1
P09121	1.12e-21	47	672	32	567	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 38-2) OX=1412 GN=cgt 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
0.021323	0.594736	0.382658	0.000549	0.000348	0.000365

TMHMM  Annotations     

start	end
13	35