CAZyme Information: MGYG000000431_00922

Basic Information

• Species: CAG-288 sp000437395
• Lineage: Bacteria; Firmicutes; Bacilli; RFN20; CAG-288; CAG-288; CAG-288 sp000437395
• CAZyme ID: MGYG000000431_00922
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
526	MGYG000000431_2|CGC2	58877.52	4.4711

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000431	1700744	MAG	Sweden	Europe

• Gene Location: Start: 164444; End: 166024 Strand: -

Full Sequence      

MKKCFMPLVLTALVLSGCNPSRGKGIVEDDLIKHNIEDKYRNFYEIFVYSYCDSNGDGIG
DLQGIISKLDYIQDLGYTGIWLTPIFTSSSTHKYNTTNYLEIDPSFGTMSDLESLISECH
SRNIKLILDLAINHSSRSNAYFQKAVQAHSISKSGSTLPDTLKGYEDLYSFYDTAEEASN
ANTERSPQIVPGQDFYYECNFDNDMPEFNMDSEMFWNIAEEIMSFYLNKGIDGFRLDAVK
YYYYNSASKTQAALSRLKEIANSIKEDNYFVAECWASSGIISGYYTNSSIDSYFWFPASV
GSHSFITSSTNLDGAYKDSYLRGYSEMLVASGDKIPAPFLSNHDMSRVGTGNEGLTKFAY
GALSMLTGSTFTYYGDEIGISASVSNSDANARTHMDWSDTNENETIDPGYGQATYKYASV
KEQLEDEGSILNYYKKANALRNCIPELQRGVLSSTFSDEEESYITMVKTYNGSSITIVMN
FSQTKSIEFNCSQLRFANSLLALRDTKINIKGDTCEIPALGIAIFR

Enzyme Prediction     

No EC number prediction in MGYG000000431_00922.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	60	381	1.4e-81	0.9904458598726115

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11316	AmyAc_bac2_AmyA	1.44e-130	41	450	1	403	Alpha amylase catalytic domain found in bacterial 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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.
cd11333	AmyAc_SI_OligoGlu_DGase	7.85e-74	43	442	5	427	Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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	3.70e-65	41	482	1	484	Glycosidase [Carbohydrate transport and metabolism].
cd11338	AmyAc_CMD	9.02e-64	60	450	53	387	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.
pfam00128	Alpha-amylase	2.45e-60	60	381	1	329	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
QOS38963.1	5.15e-117	11	526	21	543
BCN32943.1	1.78e-95	4	526	8	561
CBL34098.1	3.08e-86	12	482	18	505
CBK95784.1	3.08e-86	8	523	14	548
BCJ96999.1	3.70e-86	36	526	81	587

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7JJT_A	2.60e-84	38	501	27	490	ChainA, Alpha-amylase [Ruminococcus bromii]
7JJN_A	4.48e-82	36	526	30	522	ChainA, Glycosidases [[Eubacterium] rectale DSM 17629],7JJN_B Chain B, Glycosidases [[Eubacterium] rectale DSM 17629]
1WZA_A	1.55e-46	38	450	2	410	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
6AAV_A	3.48e-37	44	482	19	499	Crystalstructure of alpha-glucosyl transfer enzyme, XgtA at 1.72 angstrom resolution [Xanthomonas campestris],6AAV_B Crystal structure of alpha-glucosyl transfer enzyme, XgtA at 1.72 angstrom resolution [Xanthomonas campestris]
5H2T_A	8.47e-37	39	483	24	512	Structureof trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_B Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_C Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_D Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_E Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_F Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_G Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_H Structure of trehalose synthase [Thermomonospora curvata DSM 43183]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14899	3.13e-54	40	507	32	480	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
P20845	1.25e-50	38	482	37	480	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
P21332	1.24e-34	44	487	12	516	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
P07191	2.15e-33	42	381	32	402	Maltase A2 OS=Drosophila melanogaster OX=7227 GN=Mal-A2 PE=2 SV=2
O86956	1.49e-32	44	487	4	428	4-alpha-glucanotransferase OS=Thermotoga neapolitana OX=2337 GN=mgtA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000047	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000431_00922.