CAZyme Information: MGYG000001345_03714

Basic Information

• Species: Bacteroides xylanisolvens
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides xylanisolvens
• CAZyme ID: MGYG000001345_03714
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
783	MGYG000001345_36|CGC3	89604	4.5196

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001345	5913018	Isolate	not provided	not provided

• Gene Location: Start: 209686; End: 212037 Strand: +

Full Sequence      

MLLCLFTIVACSDENHEMLITGPEIPELDHEPSIEELVEGINNYPTKFKGDKQGKIWYKA
AAGDDLYGYEGDVYVHIGINDWMYVPTEWGVNEDKYKAEKVADNIWCFTLAPTVREWFGA
ENAANIQNVCILFRNDEALTDEKKTSDFFITVTGDKTFTPAPVEIAACPVEEAGIHPSAD
GTSVTFALYDLDTDNNYKDYACLIGDFNDWELSTEYQMKRDNDKHFWWYTVTGIDPAKEY
GFQYYMGSEKDGNVRIGDPYCEKVLDGSNDKYLVEQGVYPASAIQYPNGKTTGIVSVFQT
KPASYNWQVSDFKIDNPDNMVIYELLFRDFTQVGSELATGTIKEATKHLDYIKSLGVNAI
ELMPIQEFDGNNSWGYNPCYYFAMDKAYGTKEEYKQFIDECHKQGIAVLLDVVYNHATGS
HPFAKLYWNSKESKTAKNNPWFNVDAPHPFSVFHDFNHESPLVREFVKRNLKFLLEEYKF
DGFRFDLTKGFTQNKSNESTASNKDDSRIVILKDYYKTVNTTNPNAVMILEHFCNLDEES
ELAKAGMKLWHNMNESYCQSGMGESSNSDFSYMRNSGMPAEGWVNFMESHDEERVAYKQT
AFGNLQNAGLDIRMKQLGTNAAFFLTVPGPKMIWQFGELGYDYSIMYKYDGTMGTEKNTD
AKPVKWDYLTDQYRKGLYDTYSTLLKLRNDNPDLFSDNAFKDWKVSVSDWDKGRYLRLES
TTKKLVVVGNFKNEQINTGVYFGNTGDWYELNGETLNVTNSSEQPVVIPANSFKLYTNFP
VNN

Enzyme Prediction     

No EC number prediction in MGYG000001345_03714.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	339	554	1.2e-46	0.6261980830670927

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	6.51e-178	305	698	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	2.74e-50	302	488	20	190	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	5.14e-45	203	640	52	471	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	1.51e-38	175	487	25	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11313	AmyAc_arch_bac_AmyA	9.59e-38	318	694	3	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT26950.1	0.0	1	783	1	783
QDH54119.1	0.0	1	783	11	793
QRM98901.1	0.0	1	783	11	793
CBK69607.1	0.0	1	783	11	793
QUT32474.1	0.0	1	783	11	793

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EH9_A	6.37e-28	253	486	49	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	6.37e-28	253	486	49	252	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGG_A	6.37e-28	253	486	49	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	2.01e-27	253	486	49	252	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	3.58e-27	253	484	49	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
P95867	1.50e-27	253	494	50	263	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q55088	3.52e-27	253	486	50	253	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
Q44316	1.81e-24	302	515	99	284	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q8CZE8	5.03e-24	201	695	49	518	1,4-alpha-glucan branching enzyme GlgB OS=Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831) OX=221109 GN=glgB PE=3 SV=1
Q6CCT1	3.23e-23	201	486	71	333	1,4-alpha-glucan-branching enzyme OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=GLC3 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
0.033733	0.965226	0.000297	0.000283	0.000216	0.000213

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001345_03714.