CAZyme Information: MGYG000000667_01243

Basic Information

• Species: UBA7173 sp900546835
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp900546835
• CAZyme ID: MGYG000000667_01243
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
569		65125.61	6.5454

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000667	2502097	MAG	Kazakhstan	Asia

• Gene Location: Start: 67505; End: 69214 Strand: +

Full Sequence      

MNRDKTKRLPEIGKAVIYQMLPRLFGNTCEHCRPNGDINENGCGKLNDITDRVLKQIRDL
GATHVWYTGIIEHATATDYSRYGIQPDDAHVVKGKAGSPYAIKDYYDIDPDVAVDVPKRM
KEFEALVGRTHKADLRVVMDFVPNHVARRYHSDAAPAGIEDFGVNDDSTKFFDTKNNFYY
IPRQLFQPQFEIGTYTEFPAKASGNDCFNAFPTRNDWYETVKLNYGVDYGDGTCHFHPIP
STWMKMLRILRFWASKGVDAFRCDMAFMVPLDFWEWAVPQVKERYPNIEFIAEIYDVNMY
RDFLGRGHFDYLYDKVNLYDTLRDIQTHHHSAARITDCWQRIDGIGHKMLNFLENHDEQR
FASSFYAGDASKFLPSLVVSSMMSNAPYMIYAGQELGERADDAEGFSGCDGRTTIFDYWS
IPTVRRWLNGGAADGGALSTAERDLRAMYRKVLRLLNSEPAFYRGTFFDVMYVNFNNPRF
SPHHNYAFLRHADDTTIVVAVNFSGEAKDLEIKMPELAFEVMGIEPASATATDLISGRRL
KKTLSPDAPFITHIGPWGAVAWKFQKNCK

Enzyme Prediction     

No EC number prediction in MGYG000000667_01243.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	41	401	3.8e-170	0.9946666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	16	461	2	455	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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.
cd11313	AmyAc_arch_bac_AmyA	2.29e-49	15	465	5	336	Alpha amylase catalytic domain found in archaeal and 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, bacteroidetes, and proteobacteria. 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.
cd11347	AmyAc_1	4.20e-31	45	365	24	319	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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	5.87e-28	15	512	1	492	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.05e-20	16	365	1	223	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
QCD35086.1	2.91e-278	14	565	5	560
QQR07864.1	3.21e-272	14	565	5	560
ASB37124.1	3.21e-272	14	565	5	560
ANU62396.1	3.21e-272	14	565	5	560
QCD40429.1	1.00e-269	14	567	9	566

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	1.12e-19	54	395	36	313	Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
4GKL_A	2.28e-17	44	362	21	262	Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana]
6LGA_A	4.10e-11	15	272	43	248	Bombyxmori GH13 sucrose hydrolase [Bombyx mori],6LGA_B Bombyx mori GH13 sucrose hydrolase [Bombyx mori],6LGB_A Bombyx mori GH13 sucrose hydrolase complexed with glucose [Bombyx mori],6LGB_B Bombyx mori GH13 sucrose hydrolase complexed with glucose [Bombyx mori],6LGC_A Bombyx mori GH13 sucrose hydrolase complexed with 1-deoxynojirimycin [Bombyx mori],6LGC_B Bombyx mori GH13 sucrose hydrolase complexed with 1-deoxynojirimycin [Bombyx mori],6LGD_A Bombyx mori GH13 sucrose hydrolase complexed with 1,4-dideoxy-1,4-imino-D-arabinitol [Bombyx mori],6LGD_B Bombyx mori GH13 sucrose hydrolase complexed with 1,4-dideoxy-1,4-imino-D-arabinitol [Bombyx mori],6LGE_A Bombyx mori GH13 sucrose hydrolase complexed with acarbose [Bombyx mori],6LGE_B Bombyx mori GH13 sucrose hydrolase complexed with acarbose [Bombyx mori]
6LGG_A	4.10e-11	15	272	43	248	Bombyxmori GH13 sucrose hydrolase mutant E322Q complexed with sucrose [Bombyx mori],6LGG_B Bombyx mori GH13 sucrose hydrolase mutant E322Q complexed with sucrose [Bombyx mori],6LGH_A Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate [Bombyx mori],6LGH_B Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate [Bombyx mori],6LGI_A Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate complexed with fructose [Bombyx mori],6LGI_B Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate complexed with fructose [Bombyx mori]
6Y9T_A	9.11e-11	15	516	28	538	FamilyGH13_31 enzyme [Lactobacillus acidophilus NCFM],6Y9T_B Family GH13_31 enzyme [Lactobacillus acidophilus NCFM]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14898	7.06e-16	14	502	133	520	Alpha-amylase 2 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyB PE=1 SV=2
P20845	1.41e-14	37	466	52	450	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
P14899	3.08e-14	10	456	30	413	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
P39795	3.22e-12	5	289	2	218	Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2
Q2RTZ1	7.48e-10	243	400	399	547	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1) OX=269796 GN=glgE 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
0.999864	0.000151	0.000015	0.000001	0.000000	0.000007

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000667_01243.