CAZyme Information: MGYG000003187_03243

Basic Information

• Species: Leclercia adecarboxylata_C
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Leclercia; Leclercia adecarboxylata_C
• CAZyme ID: MGYG000003187_03243
• CAZy Family: GH13
• CAZyme Description: Periplasmic alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
676	MGYG000003187_12|CGC1	75729.55	5.282

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003187	4670976	MAG	United States	North America

• Gene Location: Start: 40175; End: 42205 Strand: +

Full Sequence      

MKRSALALLLLPAMASADWSAPGFPTFTAEGSGVFTAQAKLTKGIRPLTVNLDKTCWQPT
NAIKLNEMMSLKPCEGDPAQWRLFRDGDYQARIDTRSGTPTLMLTVASESEKAVTSVVRQ
CPKWDGNPLTVDVSNTFPEGSVVRDFYSKQTATVQQGKITLQPAPGSNGLLLLERAGTDK
PAPFSWQNATVYFVLTDRFENGDPGNDNSYGRHKDGMQEIGTFHGGDLKGLTSKLDYLQQ
LGVNALWISSPLEQIHGWVGGGTKGDFPHYAYHGYYTQDWTRLDANMGTEDDLRQLVDEA
HRRGIRILFDVVMNHTGYATLADMQEYQFGALYLQGDELKKTLGERWTDWKPAAGQSWHS
FNDYINFSDKTAWENWWGKQWIRTDIGDYDNPGFDDLTMSLAFLPDLKTESTTPSGLPNF
YRHKPDTGAKAVDGYTPRDYLTHWLSQWVREYGIDGFRVDTAKHVELAGWQQLKDQASDA
LKAWKAANPEKKLDDAPFWMTGESWGHGVMQSDYYRHGFDAMINFDYQEQAAKAVDCLAD
IDLTWQQMAEKLQGFNVLSYLSSHDTRLFREGDQRAAELLLLAPGSVQIFYGDESARPFG
PTGSDPLQGTRSDMNWQDISGAQAATVAHWQLLGQFRARHPAVGEGTQTTLSLPQGYGFV
REHQGDKVMVVWAGNR

Enzyme Prediction     

EC	3.2.1.98	3.2.1.60	3.2.1.-	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	226	595	1.1e-169	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	19	676	20	683	alpha-amylase; Reviewed
COG0366	AmyA	5.21e-59	189	672	1	468	Glycosidase [Carbohydrate transport and metabolism].
cd11339	AmyAc_bac_CMD_like_2	1.24e-47	190	640	4	344	Alpha amylase catalytic domain found in bacterial 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). This group of CMDs is bacterial. 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.
cd11338	AmyAc_CMD	7.31e-46	188	642	1	383	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.
cd11319	AmyAc_euk_AmyA	1.04e-45	186	477	6	223	Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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
QDK18752.1	0.0	1	676	1	676
QGU13261.1	0.0	1	676	1	676
QIK11989.1	0.0	1	676	1	676
AXF62773.1	0.0	1	676	1	676
QGU08952.1	0.0	1	676	1	676

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	2.26e-36	185	675	5	399	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	3.17e-36	174	675	28	433	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	1.42e-35	185	675	6	400	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1EA9_C	8.75e-31	183	676	124	536	Cyclomaltodextrinase[Bacillus sp. (in: Bacteria)],1EA9_D Cyclomaltodextrinase [Bacillus sp. (in: Bacteria)]
1WZK_A	9.33e-27	187	671	129	531	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZK_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	0.0	1	676	1	676	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	1.57e-32	221	658	93	541	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
Q59226	3.93e-30	183	676	124	536	Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
P21543	4.20e-29	186	479	744	959	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q08341	9.42e-27	179	671	123	533	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000267	0.999044	0.000171	0.000180	0.000161	0.000145

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003187_03243.