CAZyme Information: MGYG000001351_00920

Basic Information

• Species: Edwardsiella tarda
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Edwardsiella; Edwardsiella tarda
• CAZyme ID: MGYG000001351_00920
• CAZy Family: GH13
• CAZyme Description: Maltodextrin glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
382	MGYG000001351_83|CGC7	43177.1	7.0504

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001351	3631674	Isolate	not provided	not provided

• Gene Location: Start: 359817; End: 360965 Strand: +

Full Sequence      

MIRLRQATHDAGMRLILDGVFNHTGDSHPWFDRHRQGETGACHHPDSPQREYYTFDSAGQ
ALGWKGEASLPKLDYASPGVVDRIYRDQDSVVRHWLRPPYAIDGWRLDVVHMLGEGGSAR
ANLTHLAGIYQAVKAENPQGYVLGEHFGDARRWLQAGVEDGAMNYMGFALPLRAFLAGID
VAYQPIQLTAADCAEWMERYRAGLSQQQQLCQFNQLDSHDTARFLTLLQGNHARMRLALT
WLFTWIGVPCLYYGDEIGLAGGNDPYCRAPFPWETLRWDMTLLTLCRQLAALRRQYTALR
RGGCRVIHADEESLLFIRQWQDEHLLIAIRRTGRATLSVPYTPLLPHGTWRLLCGEGKLD
AGAQGMALDLAAESASLWLLRH

Enzyme Prediction     

EC	3.2.1.41	2.4.1.25	3.2.1.33	3.2.1.54	3.2.1.135

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	2	262	1.3e-106	0.8214285714285714

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10785	PRK10785	0.0	2	372	229	598	maltodextrin glucosidase; Provisional
cd11338	AmyAc_CMD	2.99e-115	3	303	107	388	Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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.
pfam00128	Alpha-amylase	8.08e-64	3	265	56	334	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
COG0366	AmyA	4.67e-46	1	329	79	481	Glycosidase [Carbohydrate transport and metabolism].
cd11316	AmyAc_bac2_AmyA	6.12e-33	3	302	74	403	Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. 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
ATI63398.1	1.43e-293	1	382	215	596
AKH89756.1	3.19e-290	1	382	215	596
QPR29496.1	5.51e-256	1	382	215	596
AOV97604.1	1.11e-255	1	382	215	596
AGH73040.1	1.97e-225	1	380	215	594

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5BN7_A	2.07e-156	1	379	231	605	Crystalstructure of maltodextrin glucosidase from E.coli at 3.7 A resolution [Escherichia coli K-12]
5Z0T_A	2.54e-59	15	349	259	605	Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE) [Thermoactinomyces vulgaris],5Z0T_B Thermoactinomyces vulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE) [Thermoactinomyces vulgaris]
1JI1_A	9.52e-59	15	349	259	605	CrystalStructure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 [Thermoactinomyces vulgaris],1JI1_B Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 [Thermoactinomyces vulgaris],1UH3_A Thermoactinomyces vulgaris R-47 alpha-amylase/acarbose complex [Thermoactinomyces vulgaris]
1IZK_A	1.85e-58	15	349	259	605	ChainA, amylase [Thermoactinomyces vulgaris]
1IZJ_A	3.57e-58	15	349	259	605	ChainA, amylase [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21517	7.79e-156	1	379	229	603	Maltodextrin glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=malZ PE=1 SV=5
Q60053	8.14e-58	15	349	288	634	Neopullulanase 1 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaI PE=1 SV=1
P38940	6.67e-48	9	382	233	587	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q08751	3.13e-45	3	365	224	567	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
A0A7U9P668	8.63e-45	9	370	233	575	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 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
1.000041	0.000011	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001351_00920.