CAZyme Information: MGYG000000392_01685

Basic Information

• Species: Ruminococcus_E sp003521625
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp003521625
• CAZyme ID: MGYG000000392_01685
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1158		125519.84	4.3732

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000392	2042501	MAG	Sweden	Europe

• Gene Location: Start: 43794; End: 47270 Strand: +

Full Sequence      

MKTKLTVKLISVLVALSMVICCMSFAFVDVSAVTVNDKATGSAIAGSVVENDGFTWDNAT
VYFLLTDRFKNGNTSNDHSYGRTLDKNGKPISGWDTAPGTFHGGDFAGITQAIEEGYFSD
LGVNALWISAPYEQTHGYCDSGTGHFAHYSYHGYYVLDYTETDANFGTPEEFETLVDTAH
EHGLRVIMDIVMNHCGYNTVADMEEFGFGTLLEGVTDYKYVIENVSDFNKHIDYQTSAED
WGKWWGPNWVRSGLPGYTEGGGSDFTMSLAGLPDFKTEQTTPVSIPEILKTKWTKEGTYE
EKIEKYGSSNTVTGYLTSWLAEWVRKYGVDGFRCDTAKHVEKSSWKQLKTACVDALADWR
KNNPDKPGANWQQDFWMTGEAWDKGVGYDEYYTQGGFDSMINFETWGAGVFASSRVAGLY
QRYADEINTKEDFNALSFISSHDALLTRGDTSAMIYNGSAFLLAPGGVQIYYGDESNRPM
FDGLAFDGAGGSGHSLRSDMNWDSLDQTVLAHWQKVGQFRNDHVAVGGGSNTMLSATNGV
AFARTYDKNGVSDKVAAVIGASSNADITLDVSSIWSDGQQLMNTYDHTSAIVTDGKVTFN
SGENGTILIQEPDGKPIMSVKGAAKFKGTQTVTVSLEECDSATCSIDGGNKFVVTNGSTF
EIGKTAYEGDTIKITLEATNEKGSSRSVASFYKMFESEQEPTTGDPDSTVPPQPGKIYVK
SDSAPYIYVWTGENTAQCGAWPGTQMTEKNSDGYYVMELNTTDTYNVVLNNGSDKNKSRD
FKNLNGDTYLEVPSGNYSAAKVMSGSGDEPSEKSVTFTIKPYSPSASYHLYIWDADGSVL
TGGWPGMKLTEKDADGNYIFTVNGYDKVSAIVGLGSDSKRTQDITGIIDGSCIEITSEDC
TTFKLTKPEIVLSKFQTLKKEAREVLAMTSSDYTASSWNNVSAVMTTSNELIAQGEGVAD
EALVESTLESLINAKSALVLANAGLSYAVKGKTTIVGVAVQDADITVTVNGKSYKTHSDE
ITGEFTVEATALTASSVIKVDVERKGLASETYSYNMSNGDITSYIPPTTTPPTTQPTTQP
TTPPETKPTTPSVEKGDVTGDGNINVFDATLIQRYIASIVSMTSQQMQAADVDNNGKIDI
KDATEIQRYVVGLSSALG

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	5.4e-142	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	54	558	185	678	alpha-amylase; Reviewed
COG0366	AmyA	1.64e-44	59	575	1	498	Glycosidase [Carbohydrate transport and metabolism].
cd11339	AmyAc_bac_CMD_like_2	4.07e-44	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	1.39e-41	67	525	10	383	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	1.68e-40	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	1060	56	1058
QCT06045.1	0.0	8	851	4	853
QCT06087.1	7.62e-205	31	679	30	734
CDM67955.1	1.29e-198	50	971	64	1101
CDM67952.1	4.86e-186	50	770	70	800

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	1.16e-30	55	570	5	409	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	2.08e-30	55	570	39	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	1.92e-26	50	541	1	383	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAO_A	9.62e-25	56	600	6	426	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
4JCM_A	8.85e-23	41	634	23	548	ChainA, Cyclodextrin glucanotransferase [Evansella clarkii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	4.66e-129	54	558	184	671	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	2.22e-24	92	610	85	611	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
A0A7U9P668	2.40e-22	56	565	131	541	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1
P38940	1.72e-21	56	575	131	554	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
P31746	1.02e-20	61	637	42	541	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1-1) OX=29334 GN=cgt PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.054899	0.372645	0.571044	0.000705	0.000328	0.000357

TMHMM  Annotations     

start	end
13	35