CAZyme Information: MGYG000000354_00479

Basic Information

• Species: CAG-485 sp001701295
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp001701295
• CAZyme ID: MGYG000000354_00479
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
918		101020.09	4.5908

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000354	2905675	MAG	Sweden	Europe

• Gene Location: Start: 47417; End: 50173 Strand: -

Full Sequence      

MLICILASVPALRAQVVTTVPDPLQEDSGNVVVYFHADEGNKGLAGLPSDTHIYAHTGVN
VVDNDGVTTEWKYAPAWDEDLPKYQLEYVSKDLWKLNIGDIREFYGVAPTETVKKLCFVF
RNTGGTKEGKDTDGKDIFIDVLDSGFQLAFSTTRQGSVICAPTSVRFTASTTEEADIAIY
VNDSKIGDASSSKSLQCVYKFEQQGNYTVKAVATAGGKTLEKSIPIIYVRESVAAADKTV
PPMGLTKNADGSYTFCLAAPEKESVIVIGSWDGYIGSNDYVMDYVDKEIEGATFRYFKTT
IPASVTGTEFGYYYMVDGTKAVGDPYARLVLDPYNDKYISEEVYPGKPAYPEGLVPSNTL
VAWHADGLLDYKWNIEKFKGASKDNLVIYELLFRDFTGTEGEARGNGNVRLAMDKLPYLK
ELGVNAIELLPINEFNGNNSWGYNPNFYFAIDKAYGTPQDYKEFIDRCHELGMAVILDVV
FNQSDGLHPWYQMYPIRSNPFYNQTAPHAYSVLNDWNQGYPLVAQQWDDMLKFWLSEYKV
DGFRFDLVKGLGDNTSYANSSDSGTKAYNASRVARMKRLHDAMREVNPDAYFINENLAGA
KEENEMAADGELNWANVNDAGCEYAMGYSSKASLNRMWAVRDSRTAGSTVAYLESHDEQR
LAYKQDQWGAAGIKGNHKVSMQRLGAAAAQMILVPGSHMIWQFSEMGNAQNTKDATGGNN
TSPKIVCWDLLEDPDNAGLVKSYSEMIGLRLSHPDLFAETADYTFNLGSWATGRYIKART
ADKELYVVINPNPGKSIDMEIDFRSDNNSAYYVASKSFDSEPAFDAAAKKVTVEANCYAV
IATNNLSGVEGIVSDALEATRIFAVTGGIRVVNCDGPVNVYTPDGVNVASGSGDSDIMVD
AGTYVVRAAGKTAKVVVR

Enzyme Prediction     

No EC number prediction in MGYG000000354_00479.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	409	714	3.2e-49	0.9364548494983278

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	1.64e-132	371	760	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	7.04e-46	324	707	1	360	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	8.80e-43	253	707	38	471	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.99e-36	387	708	1	259	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	9.78e-32	290	547	67	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIM10833.1	0.0	12	918	6	908
QCD35300.1	3.25e-301	1	918	8	927
QQR08212.1	4.23e-250	10	820	22	759
ANU64421.1	4.23e-250	10	820	22	759
ASB37479.1	4.23e-250	10	820	22	759

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	1.22e-25	371	556	122	295	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
3VGG_A	1.48e-24	309	588	39	294	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
1EH9_A	1.48e-24	309	588	39	294	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
1EHA_A	1.48e-24	309	588	39	294	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	4.63e-24	309	588	39	294	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P95867	6.54e-28	311	588	42	297	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q44316	1.46e-25	371	756	102	525	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q55088	8.17e-24	309	588	40	295	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
Q53238	9.68e-23	242	553	4	272	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
Q8CZE8	3.53e-22	253	801	37	569	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

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
0.012636	0.986256	0.000278	0.000303	0.000257	0.000253

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000354_00479.