CAZyme Information: MGYG000001594_02380

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A
• CAZyme ID: MGYG000001594_02380
• CAZy Family: GH13
• CAZyme Description: Amylosucrase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
284		32805.6	4.75

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001594	2676484	MAG	China	Asia

• Gene Location: Start: 1504; End: 2358 Strand: -

Full Sequence      

MASTWHTVATRDVSLLRRQLDTVAGLPRDYVFQNYLRCHDDIGWGLDYDFLENFGIQEIP
HKKYLNDFLTGSYQDSFARGELYNDDPRLGDARLCGTTASLCGIERFGFEGNEEGVARGI
RYDITLHAFMLSQSGIPVIYSGDEIGQLNDYSYKNDPEKAVDSRYLHRGDFNWDLAENRH
RPETVQGKLFPVLDKLEKARKEHSVFNSNVAFRTIDTWDSSILALVRENEEEKFIGIYNF
SEYDKVAWINEEDGMYTDLLSGRDMEARGVQIPAFGCYWLLRKK

Enzyme Prediction     

No EC number prediction in MGYG000001594_02380.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	149	3.7e-48	0.37

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	5.15e-99	1	206	331	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.
COG0366	AmyA	5.68e-05	115	260	325	505	Glycosidase [Carbohydrate transport and metabolism].
cd11356	AmyAc_Sucrose_phosphorylase-like_1	8.81e-04	6	217	259	453	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.
pfam16657	Malt_amylase_C	0.003	212	279	3	75	Maltogenic Amylase, C-terminal domain. This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyzes starch material. Maltogenic amylases are central to carbohydrate metabolism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL22253.1	9.46e-181	1	284	426	709
SNU99921.1	9.33e-127	1	284	363	649
AWY96820.1	6.01e-122	1	282	332	612
BDA10513.1	9.63e-122	1	284	356	640
QIB60618.1	3.06e-120	1	284	356	640

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7ESH_A	2.64e-43	1	280	358	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]
3UCQ_A	1.31e-42	1	242	362	604	Crystalstructure of amylosucrase from Deinococcus geothermalis [Deinococcus geothermalis DSM 11300],3UER_A Crystal structure of amylosucrase from Deinococcus geothermalis in complex with turanose [Deinococcus geothermalis DSM 11300]
4AYS_A	4.45e-42	1	243	353	601	TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans]
5N7J_A	1.21e-39	1	280	354	625	Crystalstructure of Neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides [Neisseria polysaccharea]
5N6V_A	1.56e-38	1	280	354	625	Crystalstructure of Neisseria polysaccharea amylosucrase mutant derived from Neutral genetic Drift-based engineering [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q84HD6	1.70e-37	1	280	362	633	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
Q9ZEU2	1.70e-37	1	280	362	633	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams 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
1.000074	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001594_02380.