CAZyme Information: MGYG000003835_00628

Basic Information

• Species: UBA7173 sp001915385
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp001915385
• CAZyme ID: MGYG000003835_00628
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
903	MGYG000003835_4|CGC1	99972.22	6.1395

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003835	3225656	MAG	United States	North America

• Gene Location: Start: 48305; End: 51016 Strand: +

Full Sequence      

MKRILTAFTALIMLSALSVKAAMFTPSPAPLQESSKNVVITFNAAESGVAGLQNLSTDLY
AHIGVYTNLSPNSWAHTSDWGDNADKYKLKRVGANQFQITIGDIRSYFGITKADEHVTKI
CIIARNSASNVQTSDQFIDVYPEGLYLSLTSSPANTTITKATDITFTASSTQSATLKMYV
DNKEVKSATNATSLTYTQSFSTPGAQNDVKAVATNSNGTKEVTIPVVYVKPSDQQNYPGG
MPKQGAVKNTDGSVTFCLAAPGKSSVILVGSWDDYKVLSSNTMKYQDYNGYRYFWHTVKG
LDNSTYYPYYYLVDGKYKVGDPYASLILDPHSDKWLDQDVGADVFPDCPEYPYSRFDDTI
LAVYKGDMHDTYRWQVNDFKVTNPNSLVIYELLVRDFTGTSKKADGTLRKAIEKIPELNE
LGVSAIELLPVMEFDGNNSWGYSTNAYMALDKAYGSPDDLKEFIDTCHKCGIAVILDIVF
NHTPGLHPWYAMYDAGTSPFYNKTAPHDYGVYEDIKQEYPLVEQHWVDVLTFWLTKYKVD
GFRFDLVKGLGDSNSYGSGTEAYNQSRIDRMIRLHAAMKKVKPNVIHINENLAGVQEETQ
LGNDGQYQWNNQNGNAINFIKSSSSANLRYFNAKECSRPVCSTVDYAQSHDEQWVGYEAK
NAIKSSGDRFKRLGTMVAQLMMSPGPKMMLQFDEIGYDYQLTSSNRTDPKDMPPASYYNS
NDRKGLRQNYIDLNWMRRSNPDMFDKDVTPVYTGFNNGNGVRSIRLTKGNKEIIAFINPG
TSASTVTVSATKLTAANSNLLSASRNFSGTLNGTGTSVSVSVPAHSYCVYATKDVAGVDD
IVTDEIGQNKCKVTGGQGEIIIDGEYDNVAVYNLSGIMMPTLRVAAGMYIVNVDGQVTKI
LVR

Enzyme Prediction     

No EC number prediction in MGYG000003835_00628.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	404	698	1.7e-43	0.9331103678929766

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	6.63e-107	372	744	1	387	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	2.82e-48	369	696	20	360	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	9.85e-47	254	696	38	471	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	1.12e-35	294	546	70	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11341	AmyAc_Pullulanase_LD-like	3.14e-34	388	586	4	222	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
QCD35300.1	5.22e-233	1	903	1	927
QIM10833.1	4.12e-212	22	903	8	908
QQR08212.1	9.18e-168	21	779	26	730
ANU64421.1	9.18e-168	21	779	26	730
ASB37479.1	9.18e-168	21	779	26	730

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	2.37e-29	371	696	121	460	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1EH9_A	7.42e-22	375	554	90	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	7.42e-22	375	554	90	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	7.42e-22	375	554	90	261	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	2.30e-21	375	554	90	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	4.43e-23	318	554	52	264	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q9AJN6	1.49e-22	319	555	19	260	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 GN=treZ PE=3 SV=1
Q9M0S5	1.09e-21	377	550	224	433	Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 PE=1 SV=2
B9G434	1.13e-21	253	550	128	450	Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
Q44316	1.20e-21	349	555	79	277	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 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
0.000285	0.998984	0.000193	0.000175	0.000174	0.000158

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003835_00628.