CAZyme Information: MGYG000000872_01548

Basic Information

• Species: UBA7173 sp900540205
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp900540205
• CAZyme ID: MGYG000000872_01548
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
865		95263.98	4.7723

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000872	2772884	MAG	United States	North America

• Gene Location: Start: 23922; End: 26519 Strand: +

Full Sequence      

MRDFKLLCATVLAWLACAAANAQVITTNPAVVTESTKNLTITFHADWGNRGMAGLASNVK
VYAHTGVITNLSKTNADWRYCTSNWNTPQEKFRMTNAGKNLWTITIPDIREFYGVPAGET
IEKLTFVFHSTGVPAEGKTAVGGDITLTLLPENFPEPVKADFPGGNPVPGVTTNADGSAT
FCMLAPGKESVVLRGSWNDYKIVPEQQMNYTDTSDGMRYFWTTVSDVADGTDKIYYYLVD
HQMEVGDAWAKLVLDADNDKTISASVFPDMPVYPPRLVNSPTIQQSNIPLAVYNSDADKF
DWEVSDFKGVAPSDLIIYELLVRDFTGTEGQKKGNGTIRQAIDKLDYIKALGVNAVELMP
VMEFSGNQSWGYNPNFYFAPDKAYGTPDDYRQFVDECHKRGMAVIIDVVFNHADGWHPWF
NMYPPVTSPVFNAFGSAPHDYTVFNDWKQESAMVELQFEEALKYWLTAYKVDGFRFDLVK
GLGYNDSYNNPTYDAAINEWGKPSNLADLTNKYNASRVERMKKLHEAMRTVNPDAYFINE
NLAGAQEENEMAADGELNWVNVNYNSCQFAMGFQSGAELNNFYAPNYSRTWGSTVSYAES
HDEERMAYKQKTYGATGVKGNADMSMRRLGSVAAQMILTPGAHMIWQFQELGDDQTTKNA
TGGNNTGNKKVVWSLLDKPANKSLHDSYANLCKIRNSNRALFTQDAETYVTLNPWTSGRS
IALISGTRQLLLVVNPAVSGNPIEMFVPMTVDFGRLELLDASPATTPTLSAVSKRSITGL
APGAYAVYGTPEASAIESVEAEASTTGFSVEVVGGDITVTAADGRTLARNEFEVYTTTGM
QVSPEAPAKGIYIVRALGAAAKIRI

Enzyme Prediction     

No EC number prediction in MGYG000000872_01548.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	335	658	4.1e-47	0.9431438127090301

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	3.27e-127	300	705	1	390	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	1.12e-55	296	655	19	363	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	1.32e-44	180	500	39	320	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.51e-39	316	651	1	257	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.
cd11341	AmyAc_Pullulanase_LD-like	1.40e-37	314	540	2	226	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQR08212.1	9.30e-303	20	765	24	759
ANU64421.1	9.30e-303	20	765	24	759
ASB37479.1	9.30e-303	20	765	24	759
QCD35300.1	4.55e-287	15	799	14	866
QIM10833.1	6.73e-255	25	863	10	905

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	9.03e-29	228	479	50	287	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
3VGG_A	1.85e-28	232	482	39	257	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
1EH9_A	1.85e-28	232	482	39	257	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
1EHA_A	1.85e-28	232	482	39	257	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	5.86e-28	232	482	39	257	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P95867	7.80e-28	232	482	40	260	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q55088	1.02e-27	232	482	40	258	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
O22637	8.66e-23	116	503	49	438	Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 PE=1 SV=1
Q44316	2.04e-22	177	482	15	272	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q9AJN6	3.22e-22	296	482	81	255	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 GN=treZ PE=3 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
0.000549	0.994343	0.004464	0.000224	0.000193	0.000189

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000872_01548.