CAZyme Information: MGYG000002518_02140

Basic Information

• Species: Serratia surfactantfaciens
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Serratia; Serratia surfactantfaciens
• CAZyme ID: MGYG000002518_02140
• CAZy Family: GH13
• CAZyme Description: Cytoplasmic alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
496	MGYG000002518_11|CGC23	55557.84	4.5274

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002518	5076569	Isolate	India	Asia

• Gene Location: Start: 2061275; End: 2062765 Strand: +

Full Sequence      

MTKKTTLLQFFHWYYPDGGKLWREAAERASHLAELGITDLWLPPAYKGAAGGYSVGYDTY
DLFDLGEFDQKGSVATKYGDRAALEHAATTLREHGVGVLYDVVFNHKLGADEKERVHVFK
VDANNRNDIDDQGFDAMAYTRFTFPGRQGMHSEFIWDYKCFSGVDYVEQPDDKGVFKIAN
DYGDDGWNDQVDDEKGNYDYLMGADVEFRNAAVTEELKYWARWLLDTLPCDGFRLDAAKH
IPAWFFKEWADHVRDSAQRDLFIVAEYWSHDLSALQQYIELVDGKVMLFDVALHLKFHQA
SKQGDGFDMAQIFTDTLTAADPAHAVTLVANHDTQPLQSLEAPVEPWFKPLAYALILLRE
QGVPCVFYPDLYGASYRDKGRDGGEYQIDMPAIPELEKLIAARQRFANGPQTDYFDDSHC
VAFSRAGTAEAPGCVVVLTNGGESGKTVALGADLAHTAWRDFLGNRQEEITTDDQGSAHF
PVNAGSVSVWVPAASL

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	31	374	2.8e-149	0.9970760233918129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11318	AmyAc_bac_fung_AmyA	0.0	6	405	3	391	Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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.
PRK09441	PRK09441	0.0	6	491	5	479	cytoplasmic alpha-amylase; Reviewed
cd11314	AmyAc_arch_bac_plant_AmyA	8.14e-50	7	409	2	297	Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 AmyA from bacteria, archaea, water fleas, and plants. 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	2.08e-28	15	491	21	443	Glycosidase [Carbohydrate transport and metabolism].
smart00642	Aamy	4.66e-17	6	190	2	164	Alpha-amylase domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWQ46981.1	0.0	1	496	1	496
AVU39488.1	0.0	1	496	1	496
AVU34385.1	0.0	1	496	1	496
QDI51395.1	0.0	1	496	1	496
QLJ65027.1	0.0	1	496	1	496

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UZU_A	1.06e-141	6	492	7	480	Three-dimensionalstructure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
1HVX_A	1.81e-140	6	492	7	482	BACILLUSSTEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]
1UD3_A	5.34e-139	6	491	6	478	ChainA, amylase [Bacillus sp. KSM-K38]
1VJS_A	8.33e-139	6	491	6	481	StructureOf Alpha-Amylase Precursor [Bacillus licheniformis]
1OB0_A	1.67e-138	6	491	6	481	Kineticstabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26613	6.31e-252	3	491	2	490	Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 SV=3
P26612	8.81e-250	3	491	2	490	Cytoplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=amyA PE=1 SV=3
P06279	8.26e-139	6	492	41	516	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P06278	5.81e-138	6	491	35	510	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P19571	5.64e-137	6	491	41	516	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 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
1.000037	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002518_02140.