CAZyme Information: MGYG000003922_01766

Basic Information

• Species: Bacteroides sp014385165
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp014385165
• CAZyme ID: MGYG000003922_01766
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
895		100396.34	4.6963

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003922	4876803	MAG	China	Asia

• Gene Location: Start: 22217; End: 24904 Strand: -

Full Sequence      

MRRFYTLFTLLCLALFLKAQIVTTTPEFPVPGGVVSVVFDATQGNKGLMGYTGDVYAHTG
VITNLSTGDKDWRYAPDWGDNSEKYKMKSLGNNKWQLDITPDIRTYYNISDGEIIKKMAF
VFRSGDKSKEGKGEGGTDIFVAVYADGISVRMDEPVDDVVSVGENVSMKATASVVSSMKL
YLNDKVVASKDNAKEISCSYTFSDPGNYVLKAEATADGKTATDTRTLSVLGGSVEEKLPE
GVQAGANYINDTEVTLVLFAPKKSTVHVKGDFTDWKISKDYQMKKDGDNFWITLKNLEPQ
KEYFFQYVVDGAIIVADPYSEKISDVYDQYITEDTYPGLADYPTGKTEGPVTVIQTGQKK
YEWEIKNFKSVDRSNLVIYEMLFRDFTDSSNINGALEKLDYLKGLGVTAVELMPCQEFSG
NDSWGYNPNFYFAMDKAYGTTDMYKQFIDECHKRGLAVILDVVYNQADQEMPYVKMYFDG
TNPTKDNPFFNVTAPHPYSVFYDFNHESEYTKAFVKRNLKFLLEEFNLDGFRFDLTKGFT
NKQSSESTAGNFDQSRIDILKGYNAAVKAVNPNAYVILEHFCAVSEENVLAEDGMMLWRN
MNSAFRESAKGNAADFSGLYADGQSMPKESLVGFMESHDEERMGYMTGLSLTPRLKQLVC
NAAFALVVPGPKMIWQFGEMGYDVSIEYNGRTGKKPTHWEYLEDSKRKVLYDTYCKLLAL
RQSYPDLFTSSVALTMKVGTDNWSNRYLMLSKDDKHIVLVGNLGKSASDDSYQFPVAGTW
YNLMDESTIEVSSATAQVPLSAHEFRLYTNFKPVLTGVEENIAALEQFSAYYDQQRDELV
IDGEAARVEIFTISGMMVQRQDNVSILGLSVLPSGNYIARIVMNDGAVSSCKIIK

Enzyme Prediction     

No EC number prediction in MGYG000003922_01766.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	386	608	9.9e-44	0.6549520766773163

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	1.83e-174	361	730	1	389	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	7.91e-49	361	679	23	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
COG0296	GlgB	1.86e-45	245	805	27	605	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.15e-33	377	680	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.
COG1523	PulA	2.10e-30	250	535	40	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT75353.1	0.0	1	895	1	937
QDO71214.1	1.11e-315	1	895	1	944
ALJ58548.1	2.95e-315	1	895	1	942
QUT90345.1	1.19e-314	1	895	1	942
ADQ81138.1	2.95e-262	9	895	35	941

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EH9_A	5.32e-36	249	534	6	252	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
1EHA_A	5.32e-36	249	534	6	252	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGG_A	5.32e-36	249	534	6	252	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	1.72e-35	249	534	6	252	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	2.30e-35	249	532	6	250	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
Q55088	2.95e-35	249	534	7	253	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P95867	1.07e-31	249	534	7	255	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q15VD0	1.18e-23	236	727	107	616	1,4-alpha-glucan branching enzyme GlgB OS=Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) OX=342610 GN=glgB PE=3 SV=1
Q632H1	1.45e-22	245	798	19	577	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus cereus (strain ZK / E33L) OX=288681 GN=glgB PE=3 SV=1
B9J2G8	3.46e-22	245	798	27	585	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus cereus (strain Q1) OX=361100 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
0.000445	0.998706	0.000313	0.000163	0.000172	0.000174

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003922_01766.