CAZyme Information: MGYG000000484_01645

Basic Information

• Species: Butyrivibrio_A sp000431815
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Butyrivibrio_A; Butyrivibrio_A sp000431815
• CAZyme ID: MGYG000000484_01645
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
679	MGYG000000484_10|CGC1	73531.97	4.3445

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000484	2428908	MAG	Fiji	Oceania

• Gene Location: Start: 34310; End: 36349 Strand: +

Full Sequence      

MTKKKILSLILACMFVIIAAAGCGKKNNTGDEATQAGETSVESTEAGNSQNTEKPDKSSG
KNINGTILQCFAWSFNTISESMEDIAHAGYAAIQTSPANECIVGGNGGMELMGQGKWYYH
YQPTDWKIGNYQLGTKEEFKAMCEKAHSYGIKVIVDVVPNHTTGDESAVSQDLINAVGGI
DKLYHSTGKEDIKDYADRAQCTLYSQGGLYDVNTENKAFQDYFIKYLNECIACGADGFRY
DTAKHIGLEDDPKDTGVSENNFWKRVITEIDNADNIFNYGEVLQGDNERIADYIDTIGAA
TASSYGYKLRTAIKSAKMDAGDLKDYAVGSRDASTVTWVESHDTYTGEESTSLTDEDIKL
GWAFLAARENGNALFFARPYGSSADNMWGAMNRIGVAGSYLYKDATVAAANLFNKAVTGE
SEKLSNPDNDTSVIMVERGNKGLVVVNSDSSDKQINCEVSLADGKYVNRADNSTEYTVDG
GKITGTIPARSAVILCNDGYEEYGTLPEVKIEDGTSCIFNEDSIQVTLKASNADSAAYSL
NGGAETAYTDGDKIEIKAGSDNTATLRLTAKSGNNQTVMTYVFTHKATNSSGTKIYFQKP
AAWANTVNAYVYDESSSEVKENAAWPGVAMTDEGNGLYSYVLENDWSAALVIFNDGSNQY
PGTMEPGFTIENNKKYTGE

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	73	349	4.5e-97	0.9924812030075187
CBM26	594	663	2.6e-20	0.9066666666666666

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	2.62e-143	65	424	2	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	7.90e-30	65	381	2	270	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.
cd11339	AmyAc_bac_CMD_like_2	3.43e-22	119	382	80	293	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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	2.69e-21	73	293	26	257	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	2.57e-20	75	367	24	244	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBF43367.1	1.70e-167	64	676	65	594
QGX44736.1	3.14e-144	65	661	48	626
QMS95956.1	3.14e-144	65	661	48	626
QGX45717.1	3.14e-144	65	661	48	626
VTS89378.1	3.14e-144	65	661	48	626

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	3.80e-109	65	498	6	422	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UA7_A	9.13e-107	65	498	6	422	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	1.99e-106	65	498	9	425	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
3DHP_A	1.17e-17	66	485	12	460	ChainA, Alpha-amylase 1 [Homo sapiens]
1JXK_A	1.52e-17	66	485	12	455	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	3.43e-134	65	676	50	648	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P30269	1.07e-122	65	657	148	769	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P23671	2.61e-73	49	534	42	503	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
P27350	4.74e-25	71	497	42	455	Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy PE=3 SV=2
P22998	1.94e-23	71	495	41	452	Alpha-amylase OS=Streptomyces violaceus OX=1936 GN=aml 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
0.000000	0.000002	1.000051	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
7	24