CAZyme Information: MGYG000002064_01434

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873
• CAZyme ID: MGYG000002064_01434
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
927	MGYG000002064_112|CGC1	102749.21	5.1474

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002064	2319791	MAG	China	Asia

• Gene Location: Start: 3357; End: 6140 Strand: +

Full Sequence      

MKQFFTALIALVLFGIAPALAQQIVTSTPSPLQESSQGIVLTYNAASPLGNNGLKNLTTA
SDVYAHIGVITSRSTDNADWKYVVTPWPESGNDQAANTAKNRLTKTADNTYTLNIGDIRT
YFGITDRSEHVQKIALVFRNADGSKQGKTKSGGDIFVDVLFDGFALELSSDHPDNIIGAP
TTINFTVQATSAANLELLVNDKVFASKQNTTSLTAPYEFKETGYYTVKARSVYDNYTYEE
SMEISYPAGGAAATYPGGVPKMGAVKNADGSVTFCLAAPGKVSCQLVGSWNDYELSADYL
MKYQDYQGNRYFWTTVNGLANDRYYSYFYVVDDKYKVADPYAHLVLDCYSDRYERNSVWP
TRPKYPYDKFSDVMMAVYRGDLDDYKFSPFTIPAHDNLVIYELLLRDFTGIDGMSQGWGT
LKKAIEKIPYIKAMGFNAIELMPIMEFNGTNSWGYNTNFYMAPDKAYGSPTDYKDFIEAC
HKEGIAVILDIVFNQSDGLHPWYQMYPIESNPFYNKNAPHDYSVLNDWKQDNPLVQQQWT
DAIKYWMEKYNVDGFRFDLVKGLGDNGSYSSGTEAYNQSRVDRMKRLHAVIKSVKPNGIH
INENLASAREEIAMGEDGQLNWANVNDASCQFTMGWDNGNNNLFRFLASRDSRPWGSTVS
YAESHDEQRMGYKSMAYGVTGVKDGGDAYYDRLGQLAVQMLLTPGPKMVWQFGELGNDQN
TKEANGGNDTSPKLVDWRWLDDPDRHYLMETYGAVINLRMRNPELFAQTATFAPDQLSSK
FDKPRTMRLTAGDKEVIAFINPASTGAAVTVSCSASSLSASNKQLIRASKGFEPVLTGTG
TVSVSVPANGFAIFASKRVASVESVPVAGIDTDKVNVYGIRGRIVIDGDYTTASVYTLDG
RQCPSLTVPAGLYIVVVDGQASKVLVR

Enzyme Prediction     

No EC number prediction in MGYG000002064_01434.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	418	723	3.5e-46	0.9464882943143813

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	1.10e-120	390	766	8	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.
COG0296	GlgB	5.30e-49	261	778	25	527	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11325	AmyAc_GTHase	1.09e-40	393	714	33	361	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
COG1523	PulA	3.08e-36	327	666	84	469	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	6.08e-35	399	717	1	259	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCD35300.1	5.91e-283	1	927	1	927
QIM10833.1	1.69e-277	25	927	10	908
QQR08212.1	3.47e-209	15	802	18	730
ANU64421.1	3.47e-209	15	802	18	730
ASB37479.1	3.47e-209	15	802	18	730

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	1.50e-23	396	582	135	309	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
3VGG_A	2.59e-23	311	565	42	259	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	2.59e-23	311	565	42	259	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
1EHA_A	2.59e-23	311	565	42	259	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	8.06e-23	311	565	42	259	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q04KG8	2.94e-23	412	743	158	489	1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=glgB PE=3 SV=1
Q8DPS6	2.94e-23	412	743	158	489	1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=glgB PE=3 SV=1
Q97QS8	5.15e-23	412	743	158	489	1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glgB PE=3 SV=1
Q9M0S5	5.46e-23	383	563	224	433	Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 PE=1 SV=2
Q1WSM8	6.99e-23	426	757	181	513	1,4-alpha-glucan branching enzyme GlgB OS=Ligilactobacillus salivarius (strain UCC118) OX=362948 GN=glgB 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
0.000222	0.999130	0.000154	0.000172	0.000154	0.000140

TMHMM  Annotations     

start	end
7	26