CAZyme Information: MGYG000000278_00691

Basic Information

• Species: UBA3402 sp003478355
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA3402; UBA3402 sp003478355
• CAZyme ID: MGYG000000278_00691
• CAZy Family: GH13
• CAZyme Description: Amylosucrase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
286	MGYG000000278_3|CGC3	33298.37	4.4341

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000278	4338723	Isolate	China	Asia

• Gene Location: Start: 148842; End: 149702 Strand: +

Full Sequence      

MLYNVTTMATIWNTVATKDTRLLEKQLDSVYHLPGEYTFLNYLRCHDDIGWGLDYDSLGG
WGMDQVAHKQFLNDFFTGKYKESFSRGVLYNDDPVSRDARFCGTTASMCGIEEALEKQDE
GKMDQAIRLDLMLHGFMLQQSGIPVIYSGDEVGALNDNHYKEDPEKAEDSRYIHRGQFDW
KLTEKIQQEGTVQNRIFYGLRRMEEIRMEHEVFSSDALARTMDMEDDSILGILRTGETEE
MLGVYNFSDAPKKVSLQETWTDLLNDETYDTELLLKPYDFRWMIRK

Enzyme Prediction     

No EC number prediction in MGYG000000278_00691.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	156	7.2e-55	0.3875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	3.32e-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	2.28e-09	113	223	344	452	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	7.79e-08	225	282	9	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.
pfam08533	Glyco_hydro_42C	8.57e-05	234	281	7	54	Beta-galactosidase C-terminal domain. This domain is found at the C-terminus of beta-galactosidase enzymes that belong to the glycosyl hydrolase 42 family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL20810.1	5.16e-115	1	285	251	538
QCU03906.1	3.32e-113	1	285	251	538
CBL26996.1	4.17e-108	1	283	331	616
AWY96820.1	1.20e-107	1	285	325	612
QJU19083.1	3.48e-107	1	283	322	609

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3UCQ_A	5.03e-53	1	270	355	624	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	4.56e-51	1	284	346	645	TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans]
7ESH_A	1.34e-50	3	260	353	611	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	1.70e-45	3	283	349	625	Crystalstructure of Neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides [Neisseria polysaccharea]
1MVY_A	4.49e-45	3	283	349	625	ChainA, amylosucrase [Neisseria polysaccharea],1MW0_A Chain A, amylosucrase [Neisseria polysaccharea],1S46_A Chain A, amylosucrase [Neisseria polysaccharea],1ZS2_A Chain A, amylosucrase [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZEU2	2.67e-44	3	283	357	633	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
Q84HD6	2.46e-42	3	283	357	633	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
0.999984	0.000057	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000278_00691.