CAZyme Information: MGYG000000937_00664

Basic Information

• Species: UMGS403 sp900541975
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS403; UMGS403 sp900541975
• CAZyme ID: MGYG000000937_00664
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
732	MGYG000000937_5|CGC1	80779.38	4.0252

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000937	2265948	MAG	Germany	Europe

• Gene Location: Start: 16183; End: 18381 Strand: +

Full Sequence      

MISGKKRICSAVLCLLLLASSFLFTQAGARQVTMENTVLSKEDYGLAENIEDGAILHAWC
WSFDTIRENLENIARAGFTSVQTSPINACKVGDNGGMQLMGNGKWYYHYQPADYVIGNYQ
LGTKADFEALCEEAETYGIHIIVDVVANHMSSDYSVIADSIKELPGGAFHPMNGISNYNN
RQDFTQNSLLNLWDFNTQNPNVQQLILNYLKECVAAGADGFRYDAAKHIELPEDDPSFAS
DFWPVVLENGAQFQYGEILQGGADWIDVYANYMHVTASNYGGIIRNAAASANYEVSRIDN
YNANVPQDRLVTWVESHDNYCGDGSWSMLDEQQVKEAWAVITARSGGTPLFFSRPHGSST
TNQWGDNLIGAAGSDLFKNPDIAAVNSFRNTMAGLDETLRNPGGNTGVIMIERANLGAVI
VNATDQAASVETETELEDGIYYDKVTNEPYEVQNGTLTGTADAHQILVLTGEKSQTKPYV
SISQQGGNFRESLSLTVRAVNAESASYTLGGTEMPFEEEAQFEIGADMRDGDTVTVTVRA
ENAFGVTEEAYTFTKLSYPVLEGETVVYFDNQYDWESVYIYMYTENPHMDNGWPGVPMQS
IGSNMYAAVLPEEYENSRVMFSNGNGAQYPASGEPGLVIEKGQWMVYNGTWEDYKQYITP
EEEIEMGDVTGDGEVNIEDVLALQGYIAKIRTLTEAQITAGDVNYSGAIEVEDVLRMQQY
IAHMIDGFDKPV

Enzyme Prediction     

No EC number prediction in MGYG000000937_00664.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	61	323	1.2e-99	0.9887218045112782
CBM26	567	631	8.7e-17	0.88

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	2.92e-156	52	399	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	1.49e-25	53	353	2	276	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	2.57e-25	66	318	49	313	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.
cd11319	AmyAc_euk_AmyA	1.01e-22	62	273	41	246	Alpha amylase catalytic domain found in 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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.
COG0366	AmyA	2.77e-19	52	385	15	350	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWV87542.1	1.22e-164	49	632	28	620
APT17877.1	5.32e-164	3	641	5	666
QXF04715.1	1.72e-162	49	632	54	648
QIM45895.1	1.93e-158	18	630	17	626
QWX86276.1	1.11e-157	18	630	17	627

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	2.98e-129	49	469	2	419	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	2.59e-128	47	469	3	422	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1UA7_A	4.67e-128	49	469	2	419	ChainA, Alpha-amylase [Bacillus subtilis]
1XGZ_A	1.71e-16	54	459	12	464	ChainA, Alpha-amylase, pancreatic [Homo sapiens],1XH0_A Chain A, Alpha-amylase, pancreatic [Homo sapiens],1XH1_A Chain A, Alpha-amylase, pancreatic [Homo sapiens],1XH2_A Chain A, Alpha-amylase, pancreatic [Homo sapiens],3BAK_A Chain A, Pancreatic alpha-amylase [Homo sapiens],3BAX_A Chain A, Pancreatic alpha-amylase [Homo sapiens],3BAY_A Chain A, Pancreatic alpha-amylase [Homo sapiens]
1G94_A	7.44e-16	56	448	8	408	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	2.03e-148	47	653	44	650	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P30269	1.31e-128	19	628	120	772	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P23671	4.60e-79	40	499	41	491	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
O18345	1.05e-20	55	446	31	452	Alpha-amylase 2 OS=Drosophila ananassae OX=7217 GN=Amy58 PE=3 SV=2
Q9NJN7	7.83e-20	55	459	33	462	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
0.000693	0.998456	0.000251	0.000220	0.000175	0.000164

TMHMM  Annotations     

start	end
7	29