CAZyme Information: MGYG000002772_01592

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter
• CAZyme ID: MGYG000002772_01592
• CAZy Family: GH13
• CAZyme Description: Amylosucrase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
290		33871.26	4.8956

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002772	2925670	MAG	United Republic of Tanzania	Africa

• Gene Location: Start: 19; End: 891 Strand: +

Full Sequence      

MLYNVTTMATTWNSIATRDIRLLKKQMDIVSRLPKQYTFLNYLRCHDDIGWGLDFDTMKQ
WGMEEPFHKRYLNDYFTGKTEGSVSRGELYNDDPVTQDARFCGTTASMCGIEAAGFEGNA
EKMQIAIQEDLMLHAYMLTQSGIPMLYSGDELGQVNDYSYKEDAEKVSDSRYLHRGAFQW
KLADKRKDLSTVQGQLFQMLNRLEQIRRQENAFSQEAEVYTYDVHNDSILGILREYKGER
FIALFNFSEHEQTAWMQEDGIFRNLVNGEIVEVKDPVLKGYEFVWMKYKV

Enzyme Prediction     

No EC number prediction in MGYG000002772_01592.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	156	1.5e-52	0.3875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	2.37e-102	1	213	324	536	Alpha amylase catalytic domain found in Amylosucrase. Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. 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.
cd11356	AmyAc_Sucrose_phosphorylase-like_1	8.27e-07	1	227	247	456	Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do 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.
cd11343	AmyAc_Sucrose_phosphorylase-like	2.94e-05	13	219	257	445	Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do 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.
PRK14510	PRK14510	6.47e-05	109	217	485	576	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
COG0366	AmyA	9.21e-05	131	255	335	491	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL26996.1	6.16e-201	1	287	331	617
QCU03906.1	5.28e-155	1	287	251	537
CBL20810.1	7.48e-155	1	287	251	537
AWY96820.1	1.03e-151	1	287	325	611
QEK18306.1	1.10e-150	1	287	325	611

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7ESH_A	7.99e-52	3	286	353	644	ChainA, amylosucrase [Calidithermus timidus DSM 17022],7ESH_B Chain B, amylosucrase [Calidithermus timidus DSM 17022],7ESH_C Chain C, amylosucrase [Calidithermus timidus DSM 17022],7ESH_D Chain D, amylosucrase [Calidithermus timidus DSM 17022]
5N7J_A	1.34e-44	3	287	349	626	Crystalstructure of Neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides [Neisseria polysaccharea]
4AYS_A	2.14e-43	1	286	346	644	TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans]
4FLS_A	3.40e-43	3	287	349	626	Crystalstructure of Amylosucrase inactive double mutant F290K-E328Q from Neisseria polysaccharea in complex with sucrose. [Neisseria polysaccharea]
4FLQ_A	3.40e-43	3	287	349	626	Crystalstructure of Amylosucrase double mutant A289P-F290I from Neisseria polysaccharea. [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZEU2	2.01e-42	3	287	357	634	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
Q84HD6	5.27e-42	3	287	357	634	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002772_01592.