CAZyme Information: MGYG000001839_00850

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173
• CAZyme ID: MGYG000001839_00850
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
903	MGYG000001839_16|CGC1	100027.35	5.8641

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001839	2457764	MAG	Denmark	Europe

• Gene Location: Start: 4410; End: 7121 Strand: -

Full Sequence      

MKRILTAFTALIMLSVLGVKAAMFTPSPNPLQESSKNVVITFNAAESGVADLQNLSTDLY
AHIGVYTNLSPNSWAYTSTWGDNADKYKIKRVGANLFQLTIGDMRSYFGITNANEHVSKI
CIIARNSAGSVQTSDQFIDVYPEGLYVSLTTTPASTTITKATEITFTAASTQPATLKMYV
DEKEVKSATNATSLTYAHTFSTPGAQNDVKVVASNSNGTKEVSVPVVYVKPSEQQNYPGG
TPKQGAVKNADGSVTFCLAAPGKSSVIIVGSWDDYKVLSTNTMKYQDYNGYRYFWHTITG
LDNSTYYPYYYLVDGKYKVGDPYANLILDPHSDKWLDQDVGADVFPDCPEYPYTRFDDTI
LAVYKGDMHDTYRWQVNDFKVTKPNSLVIYELLVRDFTGTSKKADGTLRKAIEKIPELNE
LGVSAIELMPVMEFDGNNSWGYSTNAYMALDKAYGSPDDLKEFIDTCHKCGIAVILDIVL
NHTPGLHPWYAMYDAGTSPFYNKTAPHDYGVYEDIKQEYPLVEQHWVDVLTFWLTKYKVD
GFRFDLVKGLGDSNSYGSGTEAYNQSRIDRMIRLHAAMKKVNPNVIHINEHLASVQEETP
MGNDGQYQWNNQNGNAINFIKSSSYANLRYFNSKECSRPVCSTVDYAQSHDEQWVGYEAK
NAIKTSSNRFKRLSTMVAQLMMSPGPKMMLQFDEIGYDYQLTSANRTDPKDMPPASYYNS
NDRKGLKQSYTDLNWMRRSNPDMFDKDVIPVYTDFNNGNGVRSIRLTKGNKEIIAFINPG
TSASTVTASATKLTAANSNLLSASRNFSGTLNGTGTSVSVSVPAHSYCVYATKDVAGVDD
IVTDEIGENKCNVTGGHGEIIIDGEYDNVAVYNLSGIMMPSLKVAAGIYIVNVDGQVTKV
LVK

Enzyme Prediction     

No EC number prediction in MGYG000001839_00850.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	404	698	8.1e-44	0.9331103678929766

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	2.07e-108	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	5.92e-49	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	3.51e-46	254	696	38	471	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	3.10e-35	294	546	70	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11341	AmyAc_Pullulanase_LD-like	9.67e-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	1.34e-224	1	903	1	927
QIM10833.1	1.30e-210	22	903	8	908
QQR08212.1	2.10e-162	21	779	26	730
ANU64421.1	2.10e-162	21	779	26	730
ASB37479.1	2.10e-162	21	779	26	730

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	3.22e-30	328	696	67	460	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1EHA_A	1.80e-22	375	696	90	420	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGG_A	1.80e-22	375	696	90	420	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	2.39e-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]
3VGD_A	7.42e-22	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	3.33e-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
Q55088	1.32e-21	375	554	91	262	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
Q9AJN6	1.89e-21	319	555	19	260	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 GN=treZ PE=3 SV=1
O04196	1.96e-21	309	563	143	428	Isoamylase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA1 PE=1 SV=1
P30538	3.23e-21	248	696	33	467	1,4-alpha-glucan branching enzyme GlgB OS=Geobacillus stearothermophilus OX=1422 GN=glgB PE=1 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
0.000353	0.998948	0.000197	0.000162	0.000165	0.000155

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001839_00850.