CAZyme Information: MGYG000000707_01646

Basic Information

• Species: Prevotella sp900546575
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900546575
• CAZyme ID: MGYG000000707_01646
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
736	MGYG000000707_35|CGC2	79934.23	5.8456

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000707	3151200	MAG	Kazakhstan	Asia

• Gene Location: Start: 10860; End: 13070 Strand: -

Full Sequence      

MKKTINYGLLMLVMLFTMASNIFADNKYGLKDNIQDGVILHCFDWTLADIQAEIPNIAKA
GFSAVQTSPVHERAGKGSVWYDVYRPYDFKIGNGLGTEADLKALCAKAHEYGVKVIVDVV
ANHTDHPNVAERLKDESLYHERFGVGSWNDRHQVTFGMIGMWDLDTNNPTVQAIIRQYIQ
DLKACGVDGIRWDAIKHIGLPSEGDSFMKNVVDQEMYNYGEILDGTGGNDNVLFPEYQTY
MSITDNGYGNGFANSFAGGSINESVGNFNQRKAKTEKLVYWGESHDTYANDGGESKEKSQ
NVIDRAYAVVAGNNGATALYFSRPAQKAKNDIKFGDKGSVHFKDAEVAQVNHMHNVCAGE
PNYYVKGNGVCAQVRKSGAIIVLGSGSDRDVTVANGAGDGKWLKSGTYKDMVGGGAFTVN
ASTISGHVGESGIAVIYNAGPIVLTPEVVFNPVDGTAFSDESLTVTATPLNAVSVWIQVN
DGAKQTFTAAKQFTVGADVAYGKNVTITWGATDKDGKTETGSVTYKKVKAYVPELGKADE
ISCFLETSNAAAAVYVWNDKVSPVIQHAGAWNDAINKKLPLVGKSVSGKNVFKWTYDGTE
TTTPTQIIFLDGNGNKITADVEFVNHGYYVDGTYSTTVTKVHEDEIVDPKYVYFDNASNW
ENVYCYFYNGKTSSTTWPGVKMTYDASASHNGKTGWYKVEIPAGYTNAKFFINDGTPGTA
IDATNASTTKVVNKGK

Enzyme Prediction     

No EC number prediction in MGYG000000707_01646.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	45	291	2e-66	0.9887218045112782

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	1.18e-108	36	364	1	352	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.
cd11317	AmyAc_bac_euk_AmyA	5.57e-33	37	307	2	257	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.
cd11320	AmyAc_AmyMalt_CGTase_like	4.62e-20	44	262	45	284	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.
cd00551	AmyAc_family	5.48e-19	32	287	8	216	Alpha amylase catalytic domain family. 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; and 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 this 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	8.50e-17	23	201	11	206	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNT67433.1	0.0	1	732	1	732
QUB83913.1	8.12e-134	1	444	3	441
QFJ55411.1	2.83e-122	28	440	46	468
ASR47410.1	1.01e-90	27	617	45	630
QDY86356.1	7.52e-90	20	617	38	630

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	5.93e-69	33	437	2	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	6.43e-69	33	437	5	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1UA7_A	8.26e-69	33	437	2	420	ChainA, Alpha-amylase [Bacillus subtilis]
1G94_A	1.04e-18	40	293	6	271	CRYSTALSTRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]
1JD7_A	1.08e-18	40	293	6	271	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	8.91e-78	33	631	46	650	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P30269	6.23e-56	24	718	135	882	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P23671	1.42e-50	23	466	40	488	Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2
Q9NJN8	1.05e-19	39	258	33	280	Alpha-amylase-related protein OS=Drosophila bipectinata OX=42026 GN=Amyrel PE=3 SV=1
Q9NJN7	1.83e-18	39	258	33	280	Alpha-amylase-related protein OS=Drosophila varians OX=30050 GN=Amyrel PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000241	0.999129	0.000175	0.000152	0.000144	0.000138

TMHMM  Annotations     

start	end
5	24