CAZyme Information: MGYG000001450_02346

Basic Information

• Species: Nesterenkonia massiliensis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Nesterenkonia; Nesterenkonia massiliensis
• CAZyme ID: MGYG000001450_02346
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
490	MGYG000001450_9|CGC1	53490.84	3.7333

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001450	2641047	Isolate	not provided	Europe

• Gene Location: Start: 39530; End: 41002 Strand: +

Full Sequence      

MRHTLTGALVGSSLLAVSCVGDTQDSDSSSKLRSNGDAIVHLFQWNWDSVAEECDDFLGP
NGFGGVQVSPPQEHVVIPYAEGGNYPWWQDYQPVSYQIENTRRGTGEDFERMVETCAENG
VRIYVDAVINHMTGPGEGTGSAGTEWTQYEYPDLFGDGDAAYSRDNFGPCYEGIEDWEDK
EEVQNCQLLGLSDLDTGDPDVQDQIVRYMNELVDLGVAGFRVDAAKHIPEGDMGEIVDRL
NEVPAFGGTPHLYHEVYGDDTIPYTAYTPYGQVTNFDYMRDVAASFADGDIVDLTSISDH
GDLSSDEAVVFIDNHDTQRYEPTLTYLDEDRYYLATAFMLAHPYGTPVVMSSYDFDGNEA
EGPPSLGEVDGNPAGSITEDADCSSADWICEHRDERVTGMISFRNAVEGTDLVERAEQGS
SRVAFDRGEKGFAAFNASDDEWELSAETSLPDGTYVNVAGSGNVIVSDGEIEATLPEDGV
IALYLGGEAE

Enzyme Prediction     

EC	3.2.1.1	3.2.1.116

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	62	343	1.6e-91	0.9962825278810409

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11317	AmyAc_bac_euk_AmyA	2.79e-153	36	407	1	329	Alpha amylase catalytic domain found in bacterial and eukaryotic 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 proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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.
cd11315	AmyAc_bac1_AmyA	1.89e-65	36	411	1	349	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 Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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.
cd11320	AmyAc_AmyMalt_CGTase_like	6.10e-27	55	349	53	343	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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.
smart00642	Aamy	2.78e-25	39	136	3	99	Alpha-amylase domain.
PRK09441	PRK09441	7.48e-21	101	349	75	363	cytoplasmic alpha-amylase; Reviewed

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFR08026.1	4.35e-264	1	490	1	500
QUX27743.1	1.08e-235	35	490	52	507
ASU57558.1	7.14e-235	35	490	54	509
QYX34828.1	1.65e-234	37	490	46	499
QUX24437.1	1.65e-234	37	490	46	499

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1VIW_A	5.63e-103	34	488	8	470	TENEBRIOMOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]
1CLV_A	8.86e-102	34	488	8	470	YELLOWMEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR [Tenebrio molitor],1JAE_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE [Tenebrio molitor],1TMQ_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR [Tenebrio molitor]
1JXK_A	1.55e-98	29	490	3	479	Roleof ethe mobile loop in the mehanism of human salivary amylase [Homo sapiens],1MFU_A Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant [Homo sapiens]
3DHP_A	9.99e-98	29	490	3	484	ChainA, Alpha-amylase 1 [Homo sapiens]
1PIF_A	2.20e-96	33	490	7	484	PIGALPHA-AMYLASE [Sus scrofa],1PIG_A PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE OLIGOSACCHARIDE V-1532 [Sus scrofa],4X0N_A Porcine pancreatic alpha-amylase in complex with helianthamide, a novel proteinaceous inhibitor [Sus scrofa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29750	4.00e-157	5	485	10	482	Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam PE=1 SV=1
P56634	4.85e-101	34	488	8	470	Alpha-amylase OS=Tenebrio molitor OX=7067 PE=1 SV=1
P81641	8.35e-99	15	490	10	482	Alpha-amylase B OS=Drosophila melanogaster OX=7227 GN=Amy-d PE=3 SV=3
P09107	1.44e-98	38	488	28	488	Alpha-amylase (Fragment) OS=Tribolium castaneum OX=7070 PE=3 SV=2
P08144	3.30e-98	15	488	10	493	Alpha-amylase A OS=Drosophila melanogaster OX=7227 GN=Amy-p PE=2 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
0.000263	0.099128	0.900402	0.000062	0.000082	0.000065

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001450_02346.