CAZyme Information: MGYG000003986_01928

Basic Information

• Species: CAG-485 sp900761855
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900761855
• CAZyme ID: MGYG000003986_01928
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
940		103971.22	4.9938

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003986	2429324	MAG	United Kingdom	Europe

• Gene Location: Start: 5614; End: 8436 Strand: +

Full Sequence      

MKKSYILAAVSLLLAWLGAGAQVTSEPTPLMDNSENIVIFFHADQGNKGLAGQPASAQIY
AHTGVITNKSTSDKDWKYAPSWGDNAPKYKLEYVSPNLWKLNMGTINAYYGITDPTVVVK
KLAFVFRTADKSQEGKGPGNSDIFLNVYQTGAHIELTSTLQSPFAPVGEDVTLTAAATMA
GKIEIFQGDEVVASVDNATTLTHKFQMPSDDQSFSARLTTTSGETAASDAIRVFPLIPSA
QATYPGGVPKMGAYWYPEGTTMVPDDHGSIIFCIAAPGKQSVSVVGSWTDYEVPQLMNYQ
DYQGQRYFWYILNGHPRVNWQKPQYYYFYVDGQYKVGDPYARLVLDPWNDKYIPESVYPN
LPPYPYDKVNDVTIAVLPAYQNPGYNTYDWKVKDFKGASKDDLRIYELLFRDFTGTEGAA
NGNGTVRAAIDKIPYLKNLGINAVELLPINEFNGNISWGYNPNYYFAPDKAYGTPDDYKE
FIDRCHQEGIAVILDVVFNQADWQHPWYQMYEVGQNPFFNATAPHAYSVLNDWNQGNPLV
QKQWDDMLTYWLTEYKVDGFRFDLVKGLGDNSSYPNSGDSGTNQFNQSRIDRMHRLQQVI
EKVNPNAYFINENLAGAQEENAMAAFGQLNWANINNAGCQYAMGYSSDSSLGRMYALYDS
RTWGSTVSYLESHDEQRLAYKQNQWGVSGVKGNLTVSMQRLGSCAAQMIMAPGAHMIWMF
SEMGNDQNTKDNTGGNNTDPKIVNWDAMYVPQRADLISTYRSLHSIRQQTPELFARSASF
ESKCNASDWARGRYMISRAGDKELYTVLNPNVSGSLAVSVPFTFKDNSRYRVVLQSPGSE
VSFDAAAGVVNVPANCFVVIGTEDYSSGIDTIGTDSASSADSVYSTAGGIVIISDSDAAV
YTVGGALVASSQGAGRRELRVAPGLYIVRTATKALKLAVR

Enzyme Prediction     

No EC number prediction in MGYG000003986_01928.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	421	730	3.2e-47	0.9498327759197325

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	3.15e-132	388	776	1	389	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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 (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.
cd11325	AmyAc_GTHase	1.29e-46	388	614	23	225	Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase
COG0296	GlgB	5.12e-42	264	572	32	312	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11341	AmyAc_Pullulanase_LD-like	2.62e-37	405	632	5	247	Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. 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.
COG1523	PulA	1.41e-36	254	564	16	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIM10833.1	0.0	21	940	8	908
QCD35300.1	2.83e-300	1	895	1	888
QQR08212.1	4.87e-241	1	836	1	756
ANU64421.1	4.87e-241	1	836	1	756
ASB37479.1	4.87e-241	1	836	1	756

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	7.80e-28	382	573	118	295	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1EH9_A	3.72e-25	400	572	99	261	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	3.72e-25	400	572	99	261	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
1EHA_A	3.72e-25	400	572	99	261	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	1.16e-24	400	572	99	261	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P95867	1.19e-25	388	572	90	264	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q44316	1.52e-25	386	773	100	525	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q55088	2.05e-24	400	572	100	262	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
Q53238	2.46e-23	382	791	96	540	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
Q9M0S5	9.76e-23	385	568	210	433	Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 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
0.001958	0.993392	0.003842	0.000264	0.000251	0.000256

TMHMM  Annotations     

start	end
5	24