CAZyme Information: MGYG000001828_00212

Basic Information

• Species: UBA4951 sp900542595
• Lineage: Bacteria; Firmicutes; Bacilli; RFN20; CAG-826; UBA4951; UBA4951 sp900542595
• CAZyme ID: MGYG000001828_00212
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
880	MGYG000001828_2|CGC1	97369.92	4.3892

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001828	1066613	MAG	Denmark	Europe

• Gene Location: Start: 21230; End: 23872 Strand: +

Full Sequence      

MDYKKLLFGGAVLLSLTLTSCDTPVNSGGDGTSLGDSSYTKTEVEEYMNGLKETSDANHL
YFHYKRHENASSSYNDWDVWAWAYQPFAGEGARFDWIGRMTSSDKLSATGSATIDGFGGA
YIDIDLKDSYDGGWDASSRTMGGYNTVFEKDGQMITAIGLQIVKSESRTSDSGFWVNDGG
NLYVNLEDYALTNDDGSTSYHIFVAEDHVQEPSPMPLVNIKDPFEDDDGTNTTYGHDAYN
NVDWNVLDALQATSPKFLKGDKNGTYLQNGAGVGYQIMVSSFKDTDGDGFGDIYGITQSL
DYLEELGVDVLWLTPIQLSGSYHGYDIVDYTKVDPKYGSKASPNTKNGVPTEESAMEDYM
DLLEQAHAKGMAVIMDLVLNHTSTENIWFINSAQLEKDYRGYYQWGNHVTDSDAINEAKF
WYPYGSHVYSYYAKFGSNMPELNYSYVPTREAVVMMAKSWLQKGVDGFRLDAVKHIFMDD
EVERDSNDTIINDVVNPTLNYSSNLTKNLHFWRYFNKEIKTDFPNAFIVGENLDGHAYHV
APFYEGLDSLFDFYTYYNLTSAAAHARNTSVGESVQRFTGVTTDTGFQNFNGLYSADNDG
GDKGLAGNKHTSIKYDDTSYWDLKHVYDTYHKYRTGGKNPTSSTGYEMIVGSFTSNHDIA
RVINRIAGTGNVSGIQEQGNVTKTNYESLLKSAALVEIAELMLPGLTWIYYGDEIGMTGN
FKAGQTSTTSYADLAYRQPMKWVENGEVGDGSGTTGYQITGSGTGFAFDDINSSSLVKSV
ADRASNPHYQAIKEAANLKSGNQTLIRGLFTPYGWGNDNQTLENIMNFSRTLGNDSYTVI
INFDMNQTYEAGLGGEVAFSFNGATATKLPPQSAIVMHNV

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	291	582	1.9e-68	0.8089171974522293

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11316	AmyAc_bac2_AmyA	3.16e-98	272	792	1	390	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	6.60e-68	272	718	3	367	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.
pfam00128	Alpha-amylase	2.56e-53	291	719	1	330	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.
cd11334	AmyAc_TreS	2.63e-52	275	554	8	263	Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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.
cd11328	AmyAc_maltase	6.53e-51	272	510	8	241	Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins. Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. 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
QTH44156.1	5.10e-60	271	877	56	541
ACH26135.1	2.09e-58	250	860	39	516
QRP62991.1	1.28e-56	270	765	29	402
AYQ73280.1	2.22e-56	259	765	31	423
CDM68040.2	3.53e-56	262	879	33	528

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1WZA_A	4.07e-50	261	776	2	387	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
5M99_B	5.55e-41	273	876	6	502	FunctionalCharacterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization [Thermotoga petrophila RKU-1]
5M99_A	5.64e-41	273	876	7	503	FunctionalCharacterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization [Thermotoga petrophila RKU-1]
5ZCC_A	6.31e-37	273	476	10	204	Crystalstructure of Alpha-glucosidase in complex with maltose [Bacillus sp. (in: Bacteria)],5ZCD_A Crystal structure of Alpha-glucosidase in complex with maltotriose [Bacillus sp. (in: Bacteria)],5ZCE_A Crystal structure of Alpha-glucosidase in complex with maltotetraose [Bacillus sp. (in: Bacteria)]
5ZCB_A	6.31e-37	273	476	10	204	Crystalstructure of Alpha-glucosidase [Bacillus sp. (in: Bacteria)]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14899	6.35e-53	275	745	38	372	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
P20845	9.78e-53	247	879	23	514	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
P21332	8.66e-36	273	843	10	510	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
P29094	2.94e-35	273	843	10	511	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
O86956	5.69e-35	273	520	2	210	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	1.000065	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001828_00212.