CAZyme Information: MGYG000000678_01719

Basic Information

• Species: CAG-485 sp002491165
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp002491165
• CAZyme ID: MGYG000000678_01719
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
477		52738.34	6.6191

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000678	2629642	MAG	Kazakhstan	Asia

• Gene Location: Start: 24443; End: 25876 Strand: -

Full Sequence      

MAKNKFLLLGAGAALCIPSLAAKDRLTHDPAYTNTESILHVWSWNFPTIAQNMKQIADAG
FTMIQTSPVQACFAPEGSGKKLFSENEGNWYFYYQPTDWTIGNNILGSRQQMKEMMDSAA
KYDVKVIVDVLPNHTAFDIDAVSEGFTKAVGGRDKMYHSNGFAAIRDYNDRAQCTLEGTG
GLPDVNTENPDFQKYYMQFVNELLGMGVKGFRYDTAKHIGVHSDPVDKAAGVKVNDFWDV
ATGRKAVKGVKLAVPEDELFIYGEVLQDRNVPEKEYADYMNQTASGYGHVIREMLDKESA
NGLDIINWRHEAAPEYLTTWVESHDTYCNAHESAHLTDPQIRAAYTFITARQNGTPLFFS
RPAGSSPANVWGDNVSGARGNDNFFHPEVVAANKFRTAMKGQKEDIQVNDAGTVLLVNRG
KKGAAVINVSHSANYVDLPTTLPAGTYRDVAHGKEFKVKNGRLKGALAPYASYILMK

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	44	331	1.1e-91	0.9924812030075187

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	2.93e-129	36	404	2	350	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	8.28e-20	38	265	4	173	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.
COG0366	AmyA	8.82e-19	44	326	26	316	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	5.03e-14	49	326	6	290	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.
smart00642	Aamy	4.45e-13	49	142	21	105	Alpha-amylase domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGK84826.1	5.42e-271	4	477	2	476
QCD43159.1	2.37e-201	3	477	2	477
QCD40786.1	2.79e-195	31	475	17	464
QCP73835.1	2.79e-195	31	475	17	464
QCD35398.1	9.05e-189	31	475	30	475

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	8.68e-88	37	467	7	411	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UA7_A	2.11e-85	37	467	7	411	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	4.57e-85	37	467	10	414	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1JXK_A	1.90e-12	37	465	12	459	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]
1CLV_A	2.40e-12	37	454	12	431	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
P30269	1.55e-90	19	467	138	597	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P00691	9.53e-82	6	467	21	455	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	3.47e-56	30	467	48	452	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
P29750	4.87e-22	8	453	14	449	Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam PE=1 SV=1
P27350	3.60e-21	13	469	13	447	Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy 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
0.015195	0.624765	0.356431	0.001956	0.000913	0.000723

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000678_01719.