CAZyme Information: MGYG000001525_02032

Basic Information

• Species: Paenibacillus_A rubinfantis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A rubinfantis
• CAZyme ID: MGYG000001525_02032
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
562	MGYG000001525_18|CGC11	61737.31	4.3951

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001525	5369528	Isolate	not provided	not provided

• Gene Location: Start: 428169; End: 429857 Strand: -

Full Sequence      

MPIHNLPRRTVLRRFGSAVLILLLLAGCTGSPSGSDAASESNQPAAETPADSSQNAKADA
VDPQPSTVFYEVFVRSFADSNGDGIGDFKGLTSKLDYLNDGNPDTDTDLGIGGIWLMPIN
PSPSYHGYDVTDYRNINPEYGTLDDFRTFMEEAHKRGIKVIMDLVVNHTSKEHPWFTESA
ADPSSPYRDWYVWAEDSGRATSGSSAAGSGNPWHSLRGDHYLGIFWEGMPDLNFDNPEVR
KEMIETGKFWLEQGLDGFRLDAAKHIYEDLQTDKSQETTNKNVAWWQEFRSGLNETKPDV
YLVGEVWDPSAALISSYLDGALDSGFNFSLAETILSSVKNEKDANIPFTLERTYKLYSEK
SSGTFVDATFLTNHDQNRVMTQLEGDVPHAKMAASLLLTLPGNPFIYYGEEIGMFGAKPD
ELIREPMRWTQDDSEGQTTWEAAENNAGKKGLSVSEQTGNSDSLLSHYRKLIRMRNGIPA
LKDGAIQEYPTDQPGITAYVRVTEDQAVLVAHNLTGSELTFTLGPGQAGGKNFTQVLAET
GEGTGLSGNTLTLPAYSTAILE

Enzyme Prediction     

EC	3.2.1.1	3.2.1.54

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	86	416	1.5e-131	0.9936305732484076

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11316	AmyAc_bac2_AmyA	0.0	68	484	2	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	2.20e-136	66	476	2	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.
cd11334	AmyAc_TreS	5.66e-114	65	475	3	447	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.
TIGR02456	treS_nterm	8.58e-108	66	523	5	497	trehalose synthase. Trehalose synthase interconverts maltose and alpha, alpha-trehalose by transglucosylation. This is one of at least three mechanisms for biosynthesis of trehalose, an important and widespread compatible solute. However, it is not driven by phosphate activation of sugars and its physiological role may tend toward trehalose degradation. This view is accentuated by numerous examples of fusion to a probable maltokinase domain. The sequence region described by this model is found both as the whole of a trehalose synthase and as the N-terminal region of a larger fusion protein that includes trehalose synthase activity. Several of these fused trehalose synthases have a domain homologous to proteins with maltokinase activity from Actinoplanes missouriensis and Streptomyces coelicolor (). [Energy metabolism, Biosynthesis and degradation of polysaccharides]
COG0366	AmyA	1.73e-102	67	537	1	505	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWV34154.1	5.89e-256	17	562	19	568
AIQ74836.1	5.11e-255	17	562	12	560
AIQ24404.1	4.82e-254	20	562	22	564
AIQ53127.1	6.66e-254	9	562	11	573
AIQ36212.1	1.48e-253	5	562	7	566

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1WZA_A	1.28e-156	69	562	7	486	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
7JJT_A	4.29e-86	69	522	32	481	ChainA, Alpha-amylase [Ruminococcus bromii]
7JJN_A	1.03e-83	70	562	38	522	ChainA, Glycosidases [[Eubacterium] rectale DSM 17629],7JJN_B Chain B, Glycosidases [[Eubacterium] rectale DSM 17629]
5H2T_A	7.07e-82	68	515	27	511	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]
5M99_B	7.34e-81	68	513	6	452	FunctionalCharacterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization [Thermotoga petrophila RKU-1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20845	5.68e-171	68	515	41	480	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
P14899	2.84e-147	66	521	34	462	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
P29094	6.18e-80	68	523	10	520	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
P21332	1.37e-75	67	523	9	519	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
P39795	1.47e-75	68	523	13	518	Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as TATLIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000001	0.000024	0.447853	0.000013	0.552120	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001525_02032.