CAZyme Information: MGYG000002560_03439

Basic Information

• Species: Phocaeicola sp902388365
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp902388365
• CAZyme ID: MGYG000002560_03439
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
481	MGYG000002560_29|CGC1	55278.64	4.5983

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002560	5390440	MAG	China	Asia

• Gene Location: Start: 11460; End: 12905 Strand: +

Full Sequence      

MENGVMMQYFEWNLPNDGKLWKQLKEDASHLHDIGVTAVWIPPAYKADEQQDEGYATYDL
YDLGEFDQKGTVRTKYGTKQELKEMIDELHKNHISVYLDVVLNHKAGGDFTEKIMVVEVD
PKERNKPLGEPFEIQGWTGYSFHGRKDKYSDFKWHWYHFSGTGFDDAQKRSGIFQIQGEG
KAWSQGVDGENGNYDFLLCNDIDLDHPEVVAELNRWGKWVSNELNLDGMRLDAIKHMKDK
FIAQFLDAIRSERGNDFYAVGEYWNGDLETLDAYIETVKHKVNLFDVPLHYNMFQASQEG
KDYDLQNILKNTLVEHHCDLAVTFVDNHDSQLGSSLESQIADWFKPLAYGLILLMKDGYP
CLFYGDYYGIKGEKSPHTKIIDILLDARRRYAYGEQIEYFDHPSTIGFIRTGDEEHDGSG
LVFLMSNDEAGSKKMSLGEVHKGEVWYEITGSIPEEVTLDEEGNGDFSVEGRNLAVWVKK
S

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	30	370	1.1e-149	0.9970760233918129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
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.
PRK09441	PRK09441	0.0	1	478	1	479	cytoplasmic alpha-amylase; Reviewed
cd11314	AmyAc_arch_bac_plant_AmyA	2.78e-47	5	392	1	295	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.
smart00642	Aamy	7.12e-26	5	110	2	100	Alpha-amylase domain.
cd11319	AmyAc_euk_AmyA	1.52e-25	33	376	54	341	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
QIU95208.1	0.0	1	481	1	481
ALJ42831.1	0.0	1	480	1	480
AAO79795.1	0.0	1	480	1	480
QMW86996.1	0.0	1	480	1	480
QUT42698.1	0.0	1	480	1	480

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1W9X_A	1.97e-191	3	480	2	481	ChainA, Alpha Amylase [Sutcliffiella halmapala]
2GJP_A	2.26e-191	3	480	6	485	ChainA, alpha-amylase [Sutcliffiella halmapala],2GJR_A Chain A, alpha-amylase [Sutcliffiella halmapala]
1E3X_A	1.14e-188	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	3.24e-188	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]
6GXV_A	2.94e-184	2	480	5	484	Amylasein complex with acarbose [Alicyclobacillus sp.],6GXV_B Amylase in complex with acarbose [Alicyclobacillus sp.],6GYA_A Amylase in complex with branched ligand [Alicyclobacillus sp.],6GYA_B Amylase in complex with branched ligand [Alicyclobacillus sp.],6GYA_C Amylase in complex with branched ligand [Alicyclobacillus sp.],6GYA_D Amylase in complex with branched ligand [Alicyclobacillus sp.]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00692	5.19e-187	3	480	33	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P06278	1.71e-182	3	480	33	512	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P19571	2.41e-181	3	480	39	518	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P06279	9.12e-179	3	480	39	517	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P26613	9.49e-131	1	478	1	490	Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 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
1.000065	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002560_03439.