CAZyme Information: MGYG000003174_00366

Basic Information

• Species: Collinsella sp900542125
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900542125
• CAZyme ID: MGYG000003174_00366
• CAZy Family: GH13
• CAZyme Description: Trehalose-6-phosphate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
196	MGYG000003174_8|CGC1	21801.27	4.4257

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003174	2220706	MAG	United States	North America

• Gene Location: Start: 1338; End: 1928 Strand: -

Full Sequence      

MATEKSSSRPWMSDAAIYQIYPRSFKDSTGSGLGDIAGITQQMDYLERLGIEAIWLSPFY
PSPLVDGGYDVADYCDVDPRLGSLDDFDDMIAAAHAHGIKVIVDIVPNHSSNQHPWFKAA
LAAGPGSPERARYIFRDGRGEHGELPPTNWNANFGGPAWTRVADGQWYLHMFTPEQPDFD
WSCPEVHAFFCDVLAF

Enzyme Prediction     

No EC number prediction in MGYG000003174_00366.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	34	196	7.4e-89	0.4575342465753425

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11332	AmyAc_OligoGlu_TS	6.87e-127	10	196	1	192	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), trehalose synthase (also called maltose alpha-D-glucosyltransferase), and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Trehalose synthase (EC 5.4.99.16) catalyzes the isomerization of maltose to produce trehalulose. 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.
cd11333	AmyAc_SI_OligoGlu_DGase	7.24e-97	14	196	2	181	Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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.
cd11331	AmyAc_OligoGlu_like	1.87e-87	10	196	1	185	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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.
cd11328	AmyAc_maltase	3.51e-86	11	196	4	190	Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins. Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. 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.
PRK10933	PRK10933	1.84e-83	10	196	6	188	trehalose-6-phosphate hydrolase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIA32881.1	8.51e-143	1	196	1	196
ATP54838.1	1.45e-133	12	196	1	185
AZH70602.1	4.12e-133	12	196	1	185
BAR05593.1	1.28e-104	4	196	23	215
AKV54985.1	8.17e-103	11	196	20	205

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7VOH_A	2.36e-55	6	196	2	190	ChainA, alpha-glucosidase QsGH13 [Qipengyuania seohaensis],7VOH_B Chain B, alpha-glucosidase QsGH13 [Qipengyuania seohaensis]
6K5P_A	1.60e-54	8	196	28	213	Structureof mosquito-larvicidal Binary toxin receptor, Cqm1 [Culex quinquefasciatus],6K5P_B Structure of mosquito-larvicidal Binary toxin receptor, Cqm1 [Culex quinquefasciatus],6K5P_C Structure of mosquito-larvicidal Binary toxin receptor, Cqm1 [Culex quinquefasciatus],6K5P_D Structure of mosquito-larvicidal Binary toxin receptor, Cqm1 [Culex quinquefasciatus]
2PWF_A	2.89e-54	10	196	4	187	ChainA, Sucrose isomerase [Paraburkholderia acidicola],2PWF_B Chain B, Sucrose isomerase [Paraburkholderia acidicola],2PWF_C Chain C, Sucrose isomerase [Paraburkholderia acidicola],2PWF_D Chain D, Sucrose isomerase [Paraburkholderia acidicola]
2PWE_A	2.89e-54	10	196	4	187	ChainA, Sucrose isomerase [Paraburkholderia acidicola],2PWE_B Chain B, Sucrose isomerase [Paraburkholderia acidicola]
2PWG_A	2.89e-54	10	196	4	187	ChainA, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWG_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWH_A Chain A, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWH_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P28904	2.32e-62	11	188	7	180	Trehalose-6-phosphate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=treC PE=1 SV=3
Q59905	5.20e-56	9	196	3	182	Glucan 1,6-alpha-glucosidase OS=Streptococcus dysgalactiae subsp. equisimilis OX=119602 GN=dexB PE=3 SV=1
Q95WY5	5.60e-56	1	196	20	212	Alpha-glucosidase OS=Culex pipiens OX=7175 GN=CPM1 PE=1 SV=1
Q17058	2.53e-54	14	196	29	211	Alpha-glucosidase OS=Apis mellifera OX=7460 PE=1 SV=1
P39795	1.28e-52	5	196	2	191	Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000060	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003174_00366.