CAZyme Information: MGYG000003144_00738

Basic Information

• Species: Aeromonas rivipollensis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Aeromonadaceae; Aeromonas; Aeromonas rivipollensis
• CAZyme ID: MGYG000003144_00738
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1069	MGYG000003144_2|CGC2	115538.54	4.8004

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003144	4456944	MAG	United States	North America

• Gene Location: Start: 121794; End: 125003 Strand: -

Full Sequence      

MARWILAAGLLGTLITAPCGAAAEWFFRGTANGWAATAMVSTDGVNYDTCQFFQGGDASG
GPRFKIDRYGNWQQSYPTADYTVTANTHYQIRINAGTQAITTTAVTSCEASGFARTLPQL
QVRGTFNGWASLPMTLVADHLWQAEAYMDGKTNQRLKFDQAGDWAINFGDSNADGVLERS
GGDILWSGTGNVRFQVNDETQAYSITPLGDDNQPPIAVITPGGVLNVAVGEALTLSGSDS
TDPDGQIASYLWSSGETTESISVSTAQAGTFTYGLTVTDDQGAKSSSSVSLVVSAPQTGG
SWYFRGTPNNWGLTAMTSEDGVTFCTEQAFGSSNPRFKVDRKGDWTEAYPAQDYKVSADT
SYRICFDSQDKTLEATPLAGADNQAPTVTATPAPGSYAEAQSITLGVSDDNDSAPRVHFT
TDGSTPTTASPRYAGQAIVASDKGSGTDLVIKTLSVDGTGNQREQSFSYQIGETPVAGGD
FRGESIYFLLTARFYDGDGSNNYYNRDRYKAGDPHWRGDFKGLIEKLDYIKDLGFTAIWV
TPPVENRSGLDYHGYHAYDFYRVDPRLESPGAGYREFIQAAHAKGIKVIQDVVINHSSQY
GLRGKTWIDRLPVKYYVPAGSSQGLINNGPYQGNLGDYASANRCDDDNPAAPDWYKARCQ
SDPAGTQPLIDPKTGASVPSAGYNPNRFFGIDAQTLDPSWYHLDGFMSGGDWENPLALQR
KHMAGDCIDLATGNQNVKDYLNGAIRQYLDMGVDAIRIDTLKHIERDELLTYVHDWQAHK
PGLFVFGENLVKGTGWGSELANDNASAVIRPWWYTRTTPNPANPRAGGDSGLSVLDFSLF
STFRDNVTKGSFGGVGGIFAMDWVYGDATKLITFFQNHDVGPDNDFKYRYGGEEGNAAMT
YNLLWTARGIPTLYYGEEVMFQAGKPQDIDGATMTVDQTGRAYFGNVLDNPATPSHPLYQ
HIKRLNQIRKAVPALQKAPMSQVNEWGSGISFVRDLSAQGSYAAVGLAANSAQQISLSGL
KNGTYRDAVTGTTVSVSNGSLSFAVPAYSARVWVLNGPGKVGADGKYLK

Enzyme Prediction     

No EC number prediction in MGYG000003144_00738.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	517	924	1e-149	0.997624703087886

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	3.74e-107	482	972	1	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.
cd11320	AmyAc_AmyMalt_CGTase_like	8.14e-60	480	971	1	389	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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	3.47e-53	486	932	6	365	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.
COG0366	AmyA	6.25e-40	486	919	3	356	Glycosidase [Carbohydrate transport and metabolism].
cd11319	AmyAc_euk_AmyA	1.00e-39	480	974	5	374	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
AHE49335.1	0.0	1	1069	1	1069
BBS87460.1	0.0	1	1069	1	1068
AVP94416.1	0.0	39	1069	1	1031
QYK83235.1	0.0	39	1069	1	1031
QJT24137.1	0.0	39	1069	1	1031

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1CGW_A	3.11e-32	480	1053	11	490	ChainA, Cyclomaltodextrin Glucanotransferase [Niallia circulans]
1QHO_A	4.13e-32	482	1053	7	490	FIVE-DOMAINALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX [Geobacillus stearothermophilus],1QHP_A Five-Domain Alpha-Amylase From Bacillus Stearothermophilus, Maltose Complex [Geobacillus stearothermophilus]
4CGT_A	6.94e-32	481	1053	12	483	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]
1A47_A	2.22e-31	486	1053	17	490	CGTASEFROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR [Thermoanaerobacterium thermosulfurigenes],1CIU_A Thermostable Cgtase From Thermoanaerobacterium Thermosulfurigenes Em1 At Ph 8.0. [Thermoanaerobacterium thermosulfurigenes]
1PEZ_A	2.26e-31	480	1053	11	490	ChainA, Cyclomaltodextrin glucanotransferase [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	8.43e-35	480	1053	743	1194	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P27036	8.40e-33	486	943	42	410	Cyclomaltodextrin glucanotransferase OS=Bacillus ohbensis OX=1481 GN=cgt PE=3 SV=2
P14014	2.69e-31	480	1053	45	523	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA PE=3 SV=1
P19531	2.71e-31	482	1053	40	523	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 SV=2
P26827	1.40e-30	486	1053	44	517	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2

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
0.000349	0.998958	0.000173	0.000193	0.000156	0.000157

TMHMM  Annotations     

start	end
5	27