CAZyme Information: MGYG000004884_00754

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; KLE1615
• CAZyme ID: MGYG000004884_00754
• CAZy Family: GH13
• CAZyme Description: Amylosucrase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
656	MGYG000004884_56|CGC1	75102.14	5.9852

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004884	2896455	MAG	China	Asia

• Gene Location: Start: 589; End: 2559 Strand: -

Full Sequence      

MIQRTGGACRPVRKQEQEKGTNAMNEQYERRFRKYYDELKWLYCELYENRMDAFLELCRR
MECRYRERKGALLALDEKRQQNPQWYMDRGMLGMMMYTDAFAGTLQGVEQKLDYISECGV
NYLHLMPLLDSPEGKSDGGYAVSDFRKVNPKLGTMEDLEHLCGSCHDRGISVCLDFVMNH
TSEEHSWAKAAKAGDPGFQAYYYFYDDFTVPAQYEQTVPQVFPTTAPGNFTWNPETGKYV
MTTFYPYQWDLNYGNPAVLNEMTDNLLFLVNQGIDVIRIDAVPYIWKQLGTNCRNLQQVH
NIVRILRIICQIVCPGVLLLGEVVMEPDKIAPYFGSVEKPECHMLYNVTTMATTWNTVAT
KDVGLLARQMGIISRLPKQYLFLNYLRCHDDIGWGLDYDWLRQFGMEEVPHKRYLNDYLT
GVYEWSWARGELYNSDPTSGDARLCGTTASLCGLEAAETLDDPARAEEALRQDLTLHGYM
FTQSGVPILYSGDEIGQFNDYSYHDDPAKREDSRYLHRGAFSWKNAALRTKAGTLQNKLF
EGLRKLEKTRAAYPVFDPDAEVSVLDTGNRSVLGIRREKNGEVLTALFSFSGRTETARIY
ETGTWINLLDKSTGSIVTGKAAGSQAAGNWQCTDRQPKGSGIVLEAFGMRWLYRRK

Enzyme Prediction     

No EC number prediction in MGYG000004884_00754.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	102	499	8e-174	0.9975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11324	AmyAc_Amylosucrase	0.0	26	556	3	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.
cd11334	AmyAc_TreS	1.07e-71	103	496	24	374	Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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	8.83e-67	120	570	38	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	3.76e-58	120	562	36	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.
COG0366	AmyA	4.68e-53	97	599	7	492	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASM70694.1	3.40e-284	26	609	10	593
AWY96820.1	7.93e-275	28	609	10	590
AHF24012.1	1.25e-274	26	655	8	615
CBK82085.1	1.18e-272	27	654	12	616
CBL26996.1	6.61e-272	15	610	3	597

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7ESH_A	6.83e-143	65	591	70	599	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	1.16e-140	65	594	70	606	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]
5N7J_A	5.05e-138	65	596	72	587	Crystalstructure of Neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides [Neisseria polysaccharea]
4AYS_A	9.17e-138	26	591	25	599	TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans]
4FLR_A	2.82e-137	65	596	72	587	Crystalstructure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZEU2	6.99e-137	65	596	80	595	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
Q84HD6	1.55e-135	65	596	80	595	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
P72235	1.19e-46	81	496	11	396	Trehalose synthase OS=Pimelobacter sp. (strain R48) OX=51662 GN=treS PE=3 SV=1
A0R6E0	4.10e-46	103	392	58	344	Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS PE=1 SV=1
P9WQ18	7.62e-45	82	392	40	352	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treS 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
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004884_00754.