CAZyme Information: MGYG000001713_02277

Basic Information

• Species: Vibrio furnissii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio furnissii
• CAZyme ID: MGYG000001713_02277
• CAZy Family: GH13
• CAZyme Description: Periplasmic alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
681	MGYG000001713_14|CGC3	76233.35	5.8468

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001713	4958658	Isolate	Japan	Asia

• Gene Location: Start: 232549; End: 234594 Strand: +

Full Sequence      

MKLSTLTLALLAVAPTVMASPNLAISTTTNSRDFPLSSEEPLVIPLTKDDYTLRITGVEG
QCEAPADQRVKFNSPIALNCGSATELPLKIRFTGEYAFSYDAKAHTLTFVRQATTSTKTE
FKRPIPNVTCEVYQGGDVTLALGNTYADGTQLKDAFTQQVVTVQQGKVTLTPSKTSGGLV
LLEPVEAKAQPFTYRNANIYFVMVDRFKNGDPSNDHSYGRKSDGKDEVGTFHGGDLKGVI
AKLDYIKSLGTDAIWLSPIVEQVRGFVGGGDSGSFPFYAYHGYWTRDFTKIDENFGVDDD
LKTLVTEAHKRGMKVLLDAVINHTGYATLADLQFDGVDVVNPRNLPKNWADWAPQAGENW
HSFHQNINYQSNHWRDWWGGDWVRAGLPGYPKPGSSDITMSLAGLPDFRTESTDYVTPPK
WLLNNPGTRVVAKDNYTVSDYLIEWQSDWVKRFGVDGYRVDTVKHVEGDVWKRLKQKASE
SLDEWRAANGQQGEPFWMMGEVWGHRAYRSPYFDDGFDALINFDIQKRMDTGAACLSQMA
MVYRDYAETLAKYPDFNPVSYMSSHDTELFYGRFKSLDMQRNAANALLLTPGAVQVYYGD
EVAREVGPYADDFHQGTRSSMNWDLDADRQALLSHWQTVGQFRHRHPAIGGGEHQVIEQK
NAYVFSRTLGDDKVVVAFVGR

Enzyme Prediction     

No EC number prediction in MGYG000001713_02277.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	234	601	5.2e-149	0.9944444444444445

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	20	681	11	682	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	8.84e-73	198	643	4	341	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	2.89e-61	199	653	4	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.
COG0366	AmyA	3.53e-61	197	679	1	469	Glycosidase [Carbohydrate transport and metabolism].
cd11319	AmyAc_euk_AmyA	2.61e-57	195	601	7	332	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
QDC94571.1	0.0	1	681	1	681
ADT88752.1	0.0	1	681	1	681
QUF70475.1	0.0	1	681	1	681
QKE36436.1	0.0	1	681	1	681
AVH34604.1	0.0	1	681	1	681

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	1.74e-53	193	677	5	396	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	4.37e-53	193	677	39	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]
4E2O_A	9.12e-48	193	677	6	397	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAO_A	1.12e-33	194	628	6	340	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
6XSJ_A	2.10e-32	178	601	12	353	ChainA, Alpha-amylase [Aspergillus oryzae],6XSJ_B Chain B, Alpha-amylase [Aspergillus oryzae],6XSV_A Chain A, Alpha-amylase [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	4.90e-190	21	681	12	675	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	1.73e-37	227	668	91	548	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
Q08341	1.31e-34	191	676	128	532	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P21543	3.71e-32	198	676	748	1141	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P0C1B4	1.15e-31	178	601	12	353	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
0.000220	0.999194	0.000145	0.000156	0.000136	0.000127

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001713_02277.