CAZyme Information: MGYG000001145_00222

Basic Information

• Species: TM7x sp900556355
• Lineage: Bacteria; Patescibacteria; Saccharimonadia; Saccharimonadales; Saccharimonadaceae; TM7x; TM7x sp900556355
• CAZyme ID: MGYG000001145_00222
• CAZy Family: GH13
• CAZyme Description: Oligo-1,6-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
528		60739.1	4.7818

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001145	729391	MAG	China	Asia

• Gene Location: Start: 92346; End: 93932 Strand: +

Full Sequence      

MKTWQDVASLYQIYPRSFLDTNGDGIGDLNGITKKLDYLSWLSIDSIWISPFFVSPLTDF
GYDIANYRAIDPTFGKMHDFQALLKKAHDLDIKVMIDLVPCHTSDQHPWFQESRSSRDNL
KRDYYIWRDGKDNSEPNNWRSLSGGSSWEFDEHTGQFYLHSFLKTQPDLNWDNPAVRTEM
KNIVRFWFDMGVDGMRVDAIWGISKDPDFKDDSPNPDFYGNPDDYGAFIHDHCKMGPHFQ
EYLQELASVCDEYDDKQMVFEFYPDDKLGDIYHQYSQILTVHPKASTFFMEYRDNEWHAK
NIEKKIENYLQSANSTTPFFCIGNHDQPRVASRLGEERARALSFLNLLTPGISVVYYGDE
IGMMNGELTADDIQDNFSPANSVVDSRDLERTPMQWNDSQFAGFSSAKPWLPVNENRTKI
NVDSEKIANDSLLNMHRKLLKLRQTLPILKNGDLSIVENTGNGFILGLKRELAGQRAYIF
INFADEKQSFSIPESAKIITSTHSVNLITVENLQMTVPGYCGVLLIVQ

Enzyme Prediction     

EC	3.2.1.20	3.2.1.-	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	27	365	9.7e-124	0.9912790697674418

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11333	AmyAc_SI_OligoGlu_DGase	0.0	8	444	3	427	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	0.0	4	453	3	450	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	5.08e-171	4	454	5	469	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.
cd11330	AmyAc_OligoGlu	1.09e-162	4	458	2	466	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.
cd11359	AmyAc_SLC3A1	2.03e-156	4	443	3	446	Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins. SLC3A1, also called Neutral and basic amino acid transport protein rBAT or NBAT, plays a role in amino acid and cystine absorption. Mutations in the gene encoding SLC3A1 causes cystinuria, an autosomal recessive disorder characterized by the failure of proximal tubules to reabsorb filtered cystine and dibasic amino acids. 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
QWQ31114.1	0.0	1	514	1	514
QJU11037.1	0.0	1	528	1	527
QLF51924.1	0.0	1	528	1	527
QJU07580.1	0.0	1	528	1	527
QJU10169.1	0.0	1	528	1	527

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2PWG_A	1.24e-113	4	498	5	523	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]
1ZJA_A	1.28e-113	4	498	6	524	ChainA, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],1ZJA_B Chain B, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],1ZJB_A Chain A, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],1ZJB_B Chain B, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],2PWD_A Chain A, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWD_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],4H8V_A Crystal structure of the trehalulose synthase MUTB in complex with trehalulose [Rhizobium sp. MX-45],4H8V_B Crystal structure of the trehalulose synthase MUTB in complex with trehalulose [Rhizobium sp. MX-45]
4H2C_A	1.28e-113	4	498	6	524	Trehalulosesynthase MutB R284C mutant [Rhizobium sp. MX-45]
4GO8_A	1.28e-113	4	498	6	524	ChainA, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],4GO8_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila]
2PWE_A	2.47e-113	4	498	5	523	ChainA, Sucrose isomerase [Paraburkholderia acidicola],2PWE_B Chain B, Sucrose isomerase [Paraburkholderia acidicola]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29094	7.84e-110	2	494	3	522	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
O06994	5.21e-107	1	493	1	523	Oligo-1,6-glucosidase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=malL PE=1 SV=1
Q9Z3R8	4.80e-105	2	493	15	517	Probable alpha-glucosidase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=aglA PE=3 SV=2
P21332	1.28e-103	2	494	3	521	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
Q17058	3.27e-103	10	488	32	513	Alpha-glucosidase OS=Apis mellifera OX=7460 PE=1 SV=1

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
1.000057	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001145_00222.