CAZyme Information: MGYG000002334_00922

Basic Information

• Species: Bifidobacterium thermophilum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium thermophilum
• CAZyme ID: MGYG000002334_00922
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
509		54733.79	5.0231

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002334	2291643	Isolate	not provided	not provided

• Gene Location: Start: 1207750; End: 1209279 Strand: +

Full Sequence      

MKQRIRTIVVAVLCIAVSAGLTVATFRTPTGVPADFDPASYRSDVIVTMFQANWKSVAKE
CTDTLGPEGVAYVQVSPPQESIKGTQWWTSYQPVSYNLNSKEGTEQEFKSMVATCKAAGV
GVIADAVINHTTGVDQGSGTGTGGSSFDAKGDFPAIGYTAKDFHTCDTDVINYTDQENVQ
DCRVSGLQDLDTSSAHVRDTLASYFAKLLKYGVAGFRVDAVKHISNTDVLAIKKLVAQKT
GRSLSDIWWMQEVIGNVSEAAAIQPKNYTRSGQVSEFQYAYQLKTFFSNSLVGGTKSIKD
ITSNLVPSGDAAIFVTNWDTERNGMTLTYRDENSYLLANAFMLAYPYSTPNIFSGYEYEK
SDDGAPGATKTSVPDTTCGTGSDWTCTQRWTAIRGMIGWHNVAGSARMTDWHDDGDNVIG
FGRGARAYIVINNGENDATVSYSTSMPAGDYCNVYASGDCSSKVHIGIDGKLNATVPAGS
AIAIHVAATPSTWHGTAARDASDPDWYGN

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	69	346	1.1e-98	0.9962825278810409

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11317	AmyAc_bac_euk_AmyA	4.03e-149	44	403	2	329	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.
cd11315	AmyAc_bac1_AmyA	3.95e-39	44	354	2	310	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.
smart00642	Aamy	5.19e-23	53	133	17	97	Alpha-amylase domain.
smart00632	Aamy_C	1.58e-22	409	489	1	81	Aamy_C domain.
cd11319	AmyAc_euk_AmyA	1.15e-17	96	225	88	212	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGH41236.1	0.0	1	509	1	509
AII76174.1	4.59e-237	23	492	28	498
AVT45185.1	2.24e-236	23	492	72	542
AJE05801.1	9.42e-234	23	492	26	496
AZH71368.1	4.91e-233	23	492	72	542

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1G94_A	1.96e-89	47	485	6	442	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]
1JD9_A	2.26e-89	47	485	6	442	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1JD7_A	2.26e-89	47	485	6	442	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1AQH_A	2.26e-89	47	485	6	442	ALPHA-AMYLASEFROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis],1AQM_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS COMPLEXED WITH TRIS [Pseudoalteromonas haloplanktis],1B0I_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis]
1KXH_A	1.09e-88	47	485	6	442	ChainA, alpha-amylase [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P22998	1.22e-114	15	489	10	457	Alpha-amylase OS=Streptomyces violaceus OX=1936 GN=aml PE=2 SV=1
P09794	3.15e-114	1	496	1	464	Alpha-amylase OS=Streptomyces limosus OX=1947 GN=aml PE=3 SV=1
P30270	1.25e-113	1	496	1	464	Alpha-amylase OS=Streptomyces griseus OX=1911 GN=amy PE=3 SV=1
P27350	1.63e-110	15	485	10	454	Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy PE=3 SV=2
P08486	1.76e-105	19	489	13	448	Alpha-amylase OS=Streptomyces hygroscopicus OX=1912 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.585134	0.380567	0.028226	0.001523	0.000667	0.003880

TMHMM  Annotations     

start	end
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