CAZyme Information: MGYG000002736_01350

Basic Information

• Species: UMGS403 sp900541565
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS403; UMGS403 sp900541565
• CAZyme ID: MGYG000002736_01350
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
909		98708.7	4.0844

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002736	2234011	MAG	Netherlands	Europe

• Gene Location: Start: 15688; End: 18417 Strand: +

Full Sequence      

MILKKTTSLILTLCMAIAMFALPAVTVSAAPEQTEATAATDYGLAEKTQDGVILHAWNWS
YNNIKANMQAIAQAGYSSVQTSPVQRPKDYSASYTDVKGQWWKLYQPISLSFSDGNTWLG
TKAEFKAMCDEAEKYGIKIIVDIVANHMADASGSGNSASNRSPQIDANIRNNNSYWHVNN
IWANDGSRYDMTQGSITQPDLNTGNSDIQQMVLSLLNTCIDLGADGFRFDAAKHIELPND
SGCGSQFWPTVINGSKSHAGGKDIFYYGEILNTASTAISNYTQYMSVTDNRTGDGILANV
NSGNASGAATSYYSIGAAPNKVVLWAESHDTYMGSSGNTSGISNAKIKQAWAMVGSRNGA
TALFFARPAAKMGDASTDTTWKDKSVAEVNKFHNYFIGQSEYLASSGSVAYNERGTTGVV
ISKLNGGGSVSLKANRMASGTYTDQITGNIFTVANGTISGTVGSDGIAVVYNAVTEPKNT
ISKQGGNFKTETLTLTLGLTNATSGTYQIDNGQIITYTDTAQITIGAGVPVGTSIRVNLT
ATDGETTTDATYTFTKVLNTSTYVYFDNSQTNWNNVYCYMYNDSGATVVENAAWPGVAMT
QNSEGLYEYEVPEELENGNVLFTAGYSGPQIPAQDEPGMVLDGFSMVYQNGQWQEYIDSN
PTDPQPTEPEPTEPQPTEPEPTEPPAGERYMLGDVTFDDEITLEDILIMQRSMAMMTTLT
QLQMTAGDVDRNGNIEIADVLEVQKYLAKMSTQYDIGKVFNDATMPTDPQPTEPQPTEPQ
PTEPEPTEPQPTEPSDSNEVTLYFSNGVSWDKVYIYAWRTSDENKNAEWPGEEMTAVGQN
SFGETIYQINIDLSQYDNVIFNNGSGQQTEDIPLTSASNNMGYYCDKNVQNAQGHYGYGT
YLFDPSYIV

Enzyme Prediction     

No EC number prediction in MGYG000002736_01350.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	59	335	1.4e-86	0.9887218045112782
CBM26	564	634	5.6e-17	0.8933333333333333
CBM26	801	871	1.4e-16	0.8933333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	9.62e-120	50	403	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	8.78e-31	51	344	2	251	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.
pfam16738	CBM26	1.43e-17	564	634	1	67	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.
pfam00128	Alpha-amylase	2.01e-17	120	350	49	307	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.
COG0366	AmyA	3.43e-17	118	279	72	248	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT06294.1	1.52e-188	4	726	5	745
CDM70432.1	3.00e-134	4	657	6	743
QDY86356.1	1.70e-130	37	643	41	642
AWB44629.1	3.45e-129	39	661	47	664
AET60999.1	5.58e-129	38	663	42	658

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	1.21e-81	49	471	4	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UA7_A	1.68e-80	49	471	4	420	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	2.55e-80	45	471	3	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1VIW_A	5.21e-17	53	289	13	244	TENEBRIOMOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]
1CLV_A	6.93e-17	53	289	13	244	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	1.41e-101	45	643	44	646	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	1.25e-69	44	484	47	477	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
P30269	6.84e-53	46	625	143	768	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P41131	7.38e-22	50	330	25	288	Alpha-amylase OS=Aeromonas hydrophila OX=644 GN=amyA PE=3 SV=1
O18345	4.60e-18	53	368	31	338	Alpha-amylase 2 OS=Drosophila ananassae OX=7217 GN=Amy58 PE=3 SV=2

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
0.000247	0.999096	0.000150	0.000192	0.000152	0.000137

TMHMM  Annotations     

start	end
7	29