CAZyme Information: MGYG000001433_02493

Basic Information

• Species: Bacteroides salyersiae
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides salyersiae
• CAZyme ID: MGYG000001433_02493
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
937	MGYG000001433_2|CGC3	105474.41	4.8909

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001433	5309986	Isolate	not provided	not provided

• Gene Location: Start: 202557; End: 205370 Strand: +

Full Sequence      

MKRSYVLLGFCIWVMFIAKAQIVTTNPAFPIEGKAVTLIFDAAQGTAGLKGYTGDVYAHT
GAITDQSEKESDWRYASDWNVNVAKYKMTSLGNNKWELNITPDVRSYYGVPAGEKILKMA
FVFRSSDGKKEGKDTGGKDIFVDIHETGLTVRFDQPSGIATLNSGETLAMKASASMVADM
KLFVGNEPIATQSNVKEITAEHTFLQAGNFEIRVEASIGGQTETATRTVNVLGETVQAPL
PANVRPGINYLSIHEATLVLQAPKKKTVHVVGDFNDWKLSPEYQLKQDGEFFWITLSGLE
REKEYAFQYVVDGTIYIADPYADKVLDPWNDSYIPSTVYPDLKPYPTGKAEGIVSVLQTG
QTPYQWQVTDFKKPDRNQLMVYEMHIRDFTSEHSFNAAKDKLPYLKQLGINAIELMPVNE
FEGNSSWGYNPSFYFAVDKYYGTKNDMRAFVDECHRQGIAVIIDLVLNHSFGQSPFYLLY
READGTPSADNPWYNQKSNIPNAALQWGYDFNHQSTYTRALVDSVAGFWMKEYKVDGFRY
DFTKGFSNTSQDTWANKYDAERIANLKRMSSEIWKRNSDAYVIIEHLTEGTTEEKELGEA
GIMLWRNMNHAYCESAMGWPDNSNFSGLYGGTSNMPVNSLMGYMESHDEERTSFKAWKWG
IESIKGGEASANPTTDNNLENRMKQLATNAAFFFTVPGPKMIWQFGELGYDYSINSNSDG
TVVDDNGAYRTDPKPLRWDYLENSARKELYNVYSKLMDLRLSYPELFSPDVIFSWKVSGN
TNWNNGRFITITSGDKRVVVVGNFTAVPGNYSVTFPQTGTWYDLMDENATLNVTSTTQSV
LVPANEFRLYTNFKPALTGIEETVVDSASLQVYYDSNLDELVINTKAVWVEIYSVNGMMV
QRQENVSSLGLSVLPSGQYVARIKDNKGEVESCKIIK

Enzyme Prediction     

No EC number prediction in MGYG000001433_02493.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	389	591	6.8e-44	0.5782747603833865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	0.0	364	770	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	2.30e-53	364	601	23	241	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	4.41e-53	262	847	44	605	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11313	AmyAc_arch_bac_AmyA	3.60e-35	380	766	6	333	Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. 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.
cd00551	AmyAc_family	2.67e-33	381	708	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT75353.1	0.0	1	937	1	937
QDO71214.1	0.0	1	937	1	944
QUT90345.1	0.0	1	937	1	942
ALJ58548.1	0.0	1	937	1	942
QIK54808.1	1.27e-311	19	937	18	908

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EHA_A	3.80e-30	283	579	33	285	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	3.80e-30	283	579	33	285	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	3.80e-30	283	579	33	285	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
3VGD_A	1.21e-29	283	579	33	285	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	2.15e-29	283	579	33	285	Crystalstructure of glycosyltrehalose trehalohydrolase (D252S) [Saccharolobus solfataricus],3VGF_A Crystal structure of glycosyltrehalose trehalohydrolase (D252S) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q632H1	1.28e-33	262	829	37	568	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus cereus (strain ZK / E33L) OX=288681 GN=glgB PE=3 SV=1
Q81K82	7.65e-33	262	829	45	576	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus anthracis OX=1392 GN=glgB PE=3 SV=1
C3PCL8	7.65e-33	262	829	45	576	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus anthracis (strain A0248) OX=592021 GN=glgB PE=3 SV=1
C3LC26	7.65e-33	262	829	45	576	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus anthracis (strain CDC 684 / NRRL 3495) OX=568206 GN=glgB PE=3 SV=1
Q72YJ3	1.02e-32	262	829	45	576	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus cereus (strain ATCC 10987 / NRS 248) OX=222523 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
0.000332	0.998961	0.000235	0.000159	0.000167	0.000155

TMHMM  Annotations     

start	end
5	24