CAZyme Information: MGYG000003293_01535

Basic Information

• Species: CAG-110 sp900544405
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110; CAG-110 sp900544405
• CAZyme ID: MGYG000003293_01535
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
714		77505.95	4.3868

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003293	2030729	MAG	Mongolia	Asia

• Gene Location: Start: 11348; End: 13492 Strand: -

Full Sequence      

MKKAICFLLVLSLAFGMSACAGNGKGGFVKTDAGLTLTRNSLTVTVDPDTGLVIGLASST
DSLEMDGIFVDAGIDEASVFSQLGYKDMSGLATYELPTLYPRMKEKTSYSVGKITVTEDG
FQIPLTCGDYTFLYKYTFYPNALGLNVELSTSADAKAAVNGVGFLVQGIHGFRLSDATFS
FPGSTPAGSISFLHANHYKTTTADYSAPAVVLQDGSKTSSVLFVDEVEKWTTGSWYKETG
DLCVGFLAAVEGYLDASAPMTVGTLYIPLQASGRTVYQNISDFWTVLGYHTPTDTTATEG
LAAIYSGHPYGTMDTGYFNRLTLAEYAQTIDSVADMGFDAMWLLPVFAHSGDNVYEPTDQ
GIIDKRYGGEQEAAVFIDRAHTLGMKVLFDFVPHGPRPVYSFAKEHEDWVSKKKDGSLQI
EWECVSMDYNNPDYAAYNQALAAHYAKDLGLDGARIDCSMGGLPNWDNAQGLRASAAGLQ
AGVTVVSSLREGFKEGGADVLLLPENFHPSPAYASVTDVFYDMPLYRCLYDLNQRGLSGR
EYAAAVTEFLNAEHQSSVSGQLKLRFLGNHDTVTWTFDAQRAQPLYGTEKAKALWMMLGW
IDGVLYIYQGDEDPAAYHLEGENLEAFFTDLIAAKREYLPNTLDTEYLQTGSAVFACRRF
DEQTSRLVLVNLSDTETTYTLSASASVLTALGNVTLAGNTVTLSPYSGAILQEG

Enzyme Prediction     

No EC number prediction in MGYG000003293_01535.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	326	612	1.3e-27	0.8963210702341137

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11313	AmyAc_arch_bac_AmyA	7.24e-24	322	638	20	330	Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. 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	5.99e-23	304	609	2	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.
pfam00128	Alpha-amylase	1.79e-15	328	612	8	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.
cd11338	AmyAc_CMD	7.08e-14	330	652	62	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.
COG0366	AmyA	2.39e-12	322	612	27	355	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHT61281.1	1.94e-140	38	684	13	652
AEE96957.1	1.43e-139	35	712	11	681
AZN42601.1	8.74e-133	70	710	48	695
AFL98102.1	1.36e-17	322	612	78	351
AIP99868.1	1.36e-17	322	612	78	351

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OT1_A	9.34e-11	328	612	356	647	ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]
3DHU_A	1.36e-10	310	612	16	313	Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
4GKL_A	1.56e-09	330	571	31	257	Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana]
2ZE0_A	2.07e-09	299	612	8	366	Alpha-glucosidaseGSJ [Geobacillus sp. HTA-462]
5A2A_A	2.26e-09	330	676	50	404	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29964	1.14e-11	330	712	178	574	Cyclomaltodextrinase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=Teth39_0676 PE=1 SV=2
L8B068	1.56e-10	311	683	260	623	Alpha-amylase MalA OS=Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1) OX=1227453 GN=malA PE=1 SV=1
Q4KCQ3	1.99e-09	324	457	284	423	1,4-alpha-glucan branching enzyme GlgB OS=Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5) OX=220664 GN=glgB PE=3 SV=1
B8CVY1	2.37e-09	321	457	167	308	1,4-alpha-glucan branching enzyme GlgB OS=Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562) OX=373903 GN=glgB PE=3 SV=1
Q2JZ21	4.50e-09	299	457	249	413	1,4-alpha-glucan branching enzyme GlgB 2 OS=Rhizobium etli (strain CFN 42 / ATCC 51251) OX=347834 GN=glgB2 PE=3 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
0.000000	0.000002	1.000062	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
7	29