CAZyme Information: MGYG000004899_00283

Basic Information

• Species: Bacteroides sp900555635
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900555635
• CAZyme ID: MGYG000004899_00283
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
866	MGYG000004899_1|CGC7	96735.1	5.2983

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004899	5396709	MAG	China	Asia

• Gene Location: Start: 373252; End: 375852 Strand: -

Full Sequence      

MRIIKQRTILSFWHLVCFSFVLVFVACSDNDEELQEYLTPASGSETIFEQGFNFGEAASS
QSVSFEAGQQWTAELSGENAGWCTINPAKGASGKSTIMVSVSKNETGKARTAQLNIVSGS
KKKEISISQAANAIVVPAGLSYTPENPDADQAITITFKADTKSPLYGYSGDVYVHIGIMS
EGTWLFVPAEWNENKDKCKMTSAGDNVWNITLGPNIREWFGSGTTAVNQLGVVFRSADGS
KKGIEEDSFIAVTDTKYEGFVPGEVKTAALPAGVVEGINVVDNSTVTLVLYDKDKNGNRK
DFAYVVGDFNKWTLSNDDKSQMYRDDASGCWWITLKGLDASKEYAFQYYVGMKQGEVTRL
ADAYTEKILDPDNDKHIPTSTYNESMAYPEGGRGIVSTFKIQKDNYNWKISNFKIEKPDQ
LVIYELHLRDFTSSNDLVGAKSKLSYLKTMGVNAIELMPVQEFDGNDSWGYNPCFFFAMD
KAYGTKAMYKQFIDACHEAGMAVILDVVYNHATGNHPFAKLYWDSSSNKTSSDNPYFNVD
APHPFSVFHDFNHESELVRKFVKRNLQFLLKEYKVDGFRFDLTKGFTQKSSNEQTAGNYD
ASRIAILKDYNTAIKATNQNAYVILEHFCDTREEQELAADGMHLWRNMNGAYCQSAIGWA
ENSSFNGMYEKTPAWVGFMESHDEERTSFKQTQDYANYALSTNLANRMKQLAVNTTFFLT
VPGPKMIWQFGELGYDISIEYNGRTGRKPIHWEYLDNADRKGLHETYTKLIALRNAHPGL
FSSSTIFSWSVDNTIQSTNWSNGRSLTAESITGEKLVVVGNFTNVAADVTFPAATGSWNN
YFTGKSETVGTKVNVPAHGYVVYTNF

Enzyme Prediction     

No EC number prediction in MGYG000004899_00283.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	431	650	4e-46	0.6389776357827476

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	0.0	406	783	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	1.04e-48	406	794	23	418	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	1.35e-46	305	838	52	577	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	1.19e-37	263	582	21	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11341	AmyAc_Pullulanase_LD-like	2.23e-36	422	582	4	198	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
ADD61516.1	0.0	1	866	1	859
QUT98185.1	0.0	21	866	1	839
QUT66828.1	0.0	1	866	1	859
BBK87558.1	0.0	1	866	1	859
QBJ19370.1	0.0	1	866	1	859

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EH9_A	3.27e-30	359	581	51	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	3.27e-30	359	581	51	252	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGG_A	3.27e-30	359	581	51	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	1.04e-29	359	581	51	252	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	1.85e-29	359	579	51	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	1.78e-31	359	590	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	1.81e-29	359	581	52	253	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
Q44316	4.28e-27	389	581	87	267	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q53238	7.29e-26	389	581	85	265	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
O52520	2.71e-23	360	780	61	516	Malto-oligosyltrehalose trehalohydrolase OS=Brevibacterium helvolum OX=1704 GN=treZ PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000090	0.005520	0.994398	0.000002	0.000003	0.000003

TMHMM  Annotations     

start	end
9	26