CAZyme Information: MGYG000002526_01250

Basic Information

• Species: Aeromonas hydrophila
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Aeromonadaceae; Aeromonas; Aeromonas hydrophila
• CAZyme ID: MGYG000002526_01250
• CAZy Family: GH13
• CAZyme Description: Periplasmic alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
702		77767.61	6.5985

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002526	5049466	Isolate	United States	North America

• Gene Location: Start: 1296305; End: 1298413 Strand: -

Full Sequence      

MRRTPSVSSLWLALLASPFFLHQAMAAEVRLYVDDQPVGAPLTLDKGAVQMTHPLTKGSH
QIRISDAGNSCGTSFGPSEAKPLPFGTAQPMDKCSKGQHFNLRVMLAGDYQFTFNPDTPS
LKVLRATKKSEFKRQPPAEPCISWDGGPVTVSLKGVWPDGTQLRDAYSGQQGVVKSGKLT
LTPSKESGGLLLLEPVKAATAAPFNWDQASVYFLLTDRFNNGDPANDHSFGRQKDGQDEV
ATWHGGDFKGLTAKLDYIKQLGINAIWITPMVEQVHGFIGGGEQGNFPFYAYHGYWALDF
TKIDPNYGDEESLKTLVDEAHKRGMRIILDVVMNHAGYATLADLQDLGLTDLTQNTGKLP
ARWNQWRPSGGLNWHGYNQFIDYQSPKWDQWWSGDWVRAGLPGYPQPGTDDVTGSVAGLP
DFLTESTKPVGLPPLLAAKQDTRAKALPNATVSDYLIAWHTDWVRRFGIDGFRADTVKHL
EPEVWARLKQAGTAALKEWKAANPTKKLDDLPFYMVGEVWDHGVAKDFWYQNGFDSLINF
DYQREFALPQAQCLASAEPTYAGYASRINQDPEFNVLSYISSHDTKLFFGDYQDVPLQRR
VASSFMLLPGGIQIYYGDESGRGLAKDGGVFDQALRSDMNWQELAGGEKAELVKHWQRLG
QFRAAHPAVAAGSHKKLADSPYAFVREKGDDKVVVVFAGRQP

Enzyme Prediction     

No EC number prediction in MGYG000002526_01250.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	246	620	5.1e-158	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	5	701	1	683	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	1.85e-66	210	666	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.
cd11319	AmyAc_euk_AmyA	1.22e-55	199	621	1	334	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.
cd11338	AmyAc_CMD	5.97e-50	217	673	10	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.
cd11340	AmyAc_bac_CMD_like_3	2.02e-49	211	639	6	370	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANT67061.1	0.0	1	702	1	702
QNF19758.1	0.0	1	702	1	702
QJT13345.1	0.0	1	702	1	702
BBT63430.1	0.0	1	702	1	702
AXV35424.1	0.0	1	702	1	702

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4E2O_A	7.14e-43	206	696	7	396	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
5A2A_A	2.64e-40	206	698	6	396	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	5.43e-40	206	698	40	430	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]
6SAO_A	6.78e-34	201	621	1	317	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
5OT1_A	5.88e-33	114	702	188	725	ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	1.53e-202	109	701	87	676	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P21543	6.85e-39	200	695	738	1141	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q05884	8.11e-33	243	702	95	567	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
Q08341	9.78e-32	203	691	127	526	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P0C1B4	5.63e-31	189	616	12	349	Alpha-amylase A type-3 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=amy3 PE=3 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
0.000375	0.998842	0.000209	0.000212	0.000173	0.000160

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002526_01250.