CAZyme Information: MGYG000002368_00558

Basic Information

• Species: Vibrio metoecus
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio metoecus
• CAZyme ID: MGYG000002368_00558
• CAZy Family: CBM34
• CAZyme Description: Intracellular maltogenic amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
285	MGYG000002368_3|CGC2	32567.69	6.7365

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002368	3946363	Isolate	United States	North America

• Gene Location: Start: 18366; End: 19223 Strand: -

Full Sequence      

MITRSSLTHLAKSADSYAYDNNTLHIRFRSAKGEVDRVTLWIGDPYIWAKGGLDGGNLGG
SDAHGWIGGTEVPMYLEGQSEHHDHWFASFVPPKKRSRYGFILHGKEGEKLLFGEKRCVD
IQDKRQADIELSNLSNFFCFPYINPKDVLKTPEWVRNTIWYQIFPERFHNGRPEISPPQV
EPWGSTPTRHNFMGGDLWGVIEKLDYLQDLGVNGLYFCPIFTANANHKYDTIDYYNVDPH
FGGNEAFRALVQEAHRRGMKVMLDAVFNHIGHQSPLWLDVVEKGG

Enzyme Prediction     

EC	3.2.1.54	3.2.1.133	3.2.1.135

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM34	8	148	3.4e-33	0.9833333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	1.01e-76	157	284	1	142	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.
PRK10785	PRK10785	1.78e-51	151	284	115	264	maltodextrin glucosidase; Provisional
smart00642	Aamy	3.06e-38	162	272	1	97	Alpha-amylase domain.
COG0366	AmyA	2.27e-37	158	284	1	116	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	9.63e-33	195	285	1	92	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATD29530.1	8.11e-220	1	284	1	284
AYC07092.1	8.11e-220	1	284	1	284
SYZ83388.1	4.67e-219	1	284	1	284
QAV06491.1	4.67e-219	1	284	1	284
QKU57634.1	4.67e-219	1	284	1	284

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1J0J_A	5.10e-81	4	284	3	262	ChainA, neopullulanase [Geobacillus stearothermophilus],1J0J_B Chain B, neopullulanase [Geobacillus stearothermophilus],1J0K_A Chain A, neopullulanase [Geobacillus stearothermophilus],1J0K_B Chain B, neopullulanase [Geobacillus stearothermophilus]
1J0H_A	5.10e-81	4	284	3	262	Crystalstructure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0H_B Crystal structure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0I_A Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus],1J0I_B Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus]
1GVI_A	1.55e-79	4	284	3	262	Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.]
1SMA_A	1.55e-79	4	284	3	262	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
7D9B_A	1.29e-63	5	283	5	270	ChainA, Alpha-glycosidase [Weissella cibaria]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O06988	1.25e-85	5	284	4	264	Intracellular maltogenic amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=bbmA PE=3 SV=2
Q9R9H8	1.76e-85	5	284	4	264	Intracellular maltogenic amylase OS=Bacillus subtilis OX=1423 GN=bbmA PE=1 SV=2
P38940	2.79e-80	4	284	3	262	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
A0A7U9P668	1.19e-78	4	284	3	262	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1
P32818	2.62e-72	4	284	3	262	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 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
1.000048	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002368_00558.