CAZyme Information: MGYG000000872_00886

Basic Information

• Species: UBA7173 sp900540205
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp900540205
• CAZyme ID: MGYG000000872_00886
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
565		64526.85	6.0555

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000872	2772884	MAG	United States	North America

• Gene Location: Start: 33753; End: 35450 Strand: +

Full Sequence      

MTHTKTSRLPEIGKAVIYQMIPRLFANTCKDCVPDGDITRNGCGKLNDITSNVLKQIRDL
GATHVWYTGVIEHAHATDYSAFGILPDDPHVVKGKAGSPYAIKDYYDIDPDVAVNVPDRM
KEFEALIDRTHRAGLRVVMDFVPNHVARQYHSDAAPAGIEDFGHNDDPTKFFAHGNNFYY
IPRQLFQPQFEIGDYTEFPAKASGNDCFNAFPSRNDWYETVKLNYGVDYGDGSCHFSPIP
STWMKMLRILRFWASKGVDAFRCDMVFMVPLDFWEWAIPQVKERYPDVEFIAEIYDVNLY
GEFLNRGHFDYLYDKVNLYDTLRDIQTHHHSAARITDCWQRIDGMGQRMLNFLENHDEQR
FASSFYAGDATRVLPSLVVSSMMSNAPFMIYAGQELGEPAADAEGFSGADGRTTIFDYWS
IPTVRRWLNNGKADGGESTPAERSLRDMYKKVLRLLNSEPALYEGEFFDVMYVNFNNPRF
SPHHNYAFLRHHGDTTLVVAVNFSDKPVQLQINIPQLAFDMMHIEPGKRMATELISGRRQ
AKTLSADTPFETQLAPWGAVVWKLK

Enzyme Prediction     

No EC number prediction in MGYG000000872_00886.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	41	401	1.5e-169	0.9946666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	16	462	2	456	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	2.79e-51	15	462	5	333	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	7.13e-34	45	467	24	389	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	3.86e-31	15	512	1	492	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	6.22e-22	44	397	1	327	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCD35086.1	1.31e-280	14	565	5	560
QCD40429.1	9.62e-274	14	565	9	564
QCP71534.1	9.62e-274	14	565	9	564
QCD41202.1	4.69e-271	14	565	5	560
QQR07864.1	6.08e-269	14	565	5	560

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	2.42e-22	44	395	27	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	5.33e-15	54	362	31	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	8.72e-14	4	287	32	258	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	8.72e-14	4	287	32	258	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]
6LGF_A	3.53e-13	4	287	32	258	Bombyxmori GH13 sucrose hydrolase mutant D247N complexed with sucrose [Bombyx mori],6LGF_B Bombyx mori GH13 sucrose hydrolase mutant D247N complexed with sucrose [Bombyx mori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14899	4.03e-14	10	466	30	426	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
Q9Z3R8	1.02e-12	15	564	21	550	Probable alpha-glucosidase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=aglA PE=3 SV=2
P39795	5.21e-11	5	397	2	371	Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2
P38940	7.17e-11	12	565	132	586	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
O16098	1.32e-10	16	269	87	285	Maltase 1 OS=Drosophila virilis OX=7244 GN=Mal-B1 PE=3 SV=2

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
0.999720	0.000309	0.000011	0.000001	0.000001	0.000003

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000872_00886.