CAZyme Information: MGYG000000322_02176

Basic Information

• Species: Odoribacter sp900544025
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Marinifilaceae; Odoribacter; Odoribacter sp900544025
• CAZyme ID: MGYG000000322_02176
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
481	MGYG000000322_65|CGC1	55835.15	4.8936

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000322	3470887	MAG	Sweden	Europe

• Gene Location: Start: 1048; End: 2493 Strand: -

Full Sequence      

MKNGVMMQYFEWNLPNDGKLWKQLKADAAHLHEIGVTAVWIPPAYKALKQDDEGYGTYDL
YDLGEFNQKETVRTKYGTRQELQEMIEELHKNQINVYLDAVMNHKAGADYSEKFMAKEVN
PDQREEDVSEPYEIEGWTGFNFPGRKGKYSDFQWHWYHFSGTDYNKANDKKGIYQIVGEN
KAWSQGVDGENGNYDFLMFADIDFDHPEVVEEMKRWGTWVSKEFNFDGMRLDAIKHINDQ
FIKHFLEAVRSERGQQFYAVGEYWKNDKDSLDEYLNQVEYEVDLFDVPLHYNMFQASQKG
RDYDLSQLLTDTLVTDHPELAVTFVDNHDSQKNSSLESQVKDWFKPLAYGLILLMKEGYP
CIFYGDYYGVKGKKSPHRMILDILLDARKKYAYGEQNNYFDHPNTVGFTRTGDDKHRGSG
VAVLLSNGEDGDKVMNVGEQHKGEVWHEITGNRKEEVTIDEQGNGKFPVSGGKLAVWVKK
D

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	30	370	4.4e-153	0.9970760233918129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09441	PRK09441	0.0	1	478	1	479	cytoplasmic alpha-amylase; Reviewed
cd11318	AmyAc_bac_fung_AmyA	0.0	3	390	1	391	Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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.
cd11314	AmyAc_arch_bac_plant_AmyA	2.59e-50	5	398	1	301	Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 from bacteria, archaea, water fleas, and plants. 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.
pfam00128	Alpha-amylase	4.84e-28	31	376	13	334	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.
cd11320	AmyAc_AmyMalt_CGTase_like	3.23e-26	21	366	46	347	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADY31382.1	2.21e-310	6	480	1	475
SNV25854.1	2.21e-310	6	480	1	475
QIX66724.1	1.48e-286	1	479	1	479
QJE27822.1	3.21e-286	1	479	1	479
QCY56071.1	4.56e-286	1	479	1	479

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1W9X_A	1.54e-200	3	480	2	481	ChainA, Alpha Amylase [Sutcliffiella halmapala]
2GJP_A	1.78e-200	3	480	6	485	ChainA, alpha-amylase [Sutcliffiella halmapala],2GJR_A Chain A, alpha-amylase [Sutcliffiella halmapala]
1E3X_A	8.94e-198	3	480	2	483	Nativestructure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.92A [Bacillus amyloliquefaciens],1E3Z_A Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A [Bacillus amyloliquefaciens],1E40_A Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A [Bacillus amyloliquefaciens],1E43_A Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A [Bacillus amyloliquefaciens]
3BH4_A	6.84e-195	3	480	2	483	Highresolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens],3BH4_B High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens]
1VJS_A	6.42e-193	3	480	4	483	StructureOf Alpha-Amylase Precursor [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00692	1.11e-193	3	480	33	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P06278	3.39e-192	3	480	33	512	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P19571	3.39e-191	3	480	39	518	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P06279	3.96e-180	3	480	39	517	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P26612	5.46e-141	1	478	1	490	Cytoplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=amyA PE=1 SV=3

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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000322_02176.