CAZyme Information: MGYG000003472_01620

Basic Information

• Species: Alistipes sp900768045
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900768045
• CAZyme ID: MGYG000003472_01620
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
866	MGYG000003472_101|CGC3	97198.32	4.525

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003472	2013664	MAG	Fiji	Oceania

• Gene Location: Start: 50128; End: 52728 Strand: +

Full Sequence      

MKKLHFLLMALFAAVIMVGCENLLPEEPNDTPTETPGETPGETPGDEPNDEPNDEPITGE
LPLISTSPAFVTEHMTEDITVILNTKGTAADGFTGELYAHTGVLTAKSTASNDWKYVLSE
WGNNIPECKLESKGNNIWHYTIKGGVRAWYGVAEEDTVTHIAFVFRSSDSKLEVKDNGSD
IFVELAKEGMAVKFLSPKHGSQYQVGDEIVVQTQQQATTSVTLYMNDVEVATSTSATLSY
TYTTTKSEDIVFKAVATNGTETIEESVAVAVLGATENAPRPSGVKNGVNINGDEATFVLF
APGKESVILLGDFNQYAPSNEYMMKRDGDYFWTTVSGLEEGVEYGYQYLVDETIKIGDPY
ATKILDPWNDKYISATTYPNLKPYPAEYTTDVVSVFEINHDEYQWVVSDFDRPKQNSLAI
YELLIRDFTTTRTIDAVTAKLDYLKTLGINAIELMPIQEFDGNDSWGYNPCYYFAADKAY
GTEEAYKRFIDECHKRGIAVIIDVVFNHATGLHPYAKMWWNSGANKTASNNPFFNVDAPH
NFSVFHDFNHTYSETVKFFDEVLTFWLEEYKVDGFRFDLTKGFVQNPSNYDASGYSSQRI
GILKHYAETIRSVENDAYIIFEHFCDDSEETELYNSVGALCWNISQMNGYMESVMGWTGG
EKSSFANFKKGRVNNIETHDEERVAYKAVTYGDSYVKNNWAVISKRLQAAYALHFLTPYP
KMMWQFGELGYDVSINANEEGKVGSGDEYRTHRKPVRWSYFQNADRRAMYDALSKIITWR
TSNQDYYGQDNLKVHRWAVGDASMGGKTLIMDRVIVVANFTNSTTSTTVSVPQTGEWTNL
LTGEKLQLGSSHTVSLAGSDYIVLVK

Enzyme Prediction     

No EC number prediction in MGYG000003472_01620.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	428	686	9.9e-47	0.7571884984025559

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	7.82e-159	403	785	1	385	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	2.18e-54	272	730	26	471	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11325	AmyAc_GTHase	1.63e-52	398	742	18	378	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
cd00551	AmyAc_family	6.73e-37	420	729	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.
COG1523	PulA	9.35e-36	275	587	13	375	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIK54808.1	4.54e-210	63	861	21	823
QIK60226.1	2.55e-209	63	861	21	823
ADQ81138.1	1.16e-197	57	863	45	853
AMC11972.1	1.23e-194	64	861	20	811
BAR52001.1	1.75e-194	64	840	21	715

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EHA_A	7.69e-31	290	590	6	264	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	7.69e-31	290	590	6	264	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	7.69e-31	290	590	6	264	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	2.45e-30	290	590	6	264	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	4.37e-30	290	590	6	264	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	4.25e-30	290	590	7	265	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P95867	1.03e-29	287	590	4	267	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q44316	7.38e-26	295	578	17	267	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q53238	6.56e-23	297	578	17	265	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
Q24VW3	5.45e-22	297	665	47	408	1,4-alpha-glucan branching enzyme GlgB OS=Desulfitobacterium hafniense (strain Y51) OX=138119 GN=glgB 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
0.000000	0.000000	1.000064	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003472_01620.