CAZyme Information: MGYG000003164_02202

Basic Information

• Species: CAG-485 sp002361235
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp002361235
• CAZyme ID: MGYG000003164_02202
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
567		64738.42	5.2179

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003164	2929430	MAG	United States	North America

• Gene Location: Start: 738; End: 2441 Strand: -

Full Sequence      

MKEKPIVYQMFPRIMTNMESECVADGSYEQNGSGKFNGLTVKTLKSIRSLGVTHVWYTGV
IEMATKTAFPGIPADNPNVVKGQAGSPYAIKDYYDVSPALAEDVDKRMDEFQALVERTHD
AGLKVLLDFVPNHTARVYHSDVAPDGIDDFGAHDNIGMFFTPNNNYYYITNQQFAPDFDL
GAEGDTPYVEFPAKATGNDCFTAFCGKTDWYETVKLNYGVDSWQHKGYYDPIPDTWLRML
HILRFWASKGIDGFRCDMVFMVPVEFWHWAIPQVKGDYPGLIFIGEIYDVSLYHTFLNYC
GFDYLYDKVNLYYTLVGIERNNVSAAQLTGCWQTVDGIGDRMLNFLENHDEVRFASPAFA
GDPMKVVPHLVVSAMMSKGPFMLYYGQELGEPARDNEGFAGDNNRTTIFDYWSLDTLRRW
YNNGLCSTAHLTAHEKWLRNLYKRVLTLCNKSAAVREGAFFDLMYVNLQQPDFDPHRLYS
FVRYTDTDVLLFLVNFADRSQDVHLNVPDLCYDMAGIAEGDYKVEDLLWKQPHVFTMQRG
QQTMLKIGPHDALILPLKKVKPTNNAK

Enzyme Prediction     

No EC number prediction in MGYG000003164_02202.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	31	394	1.1e-156	0.9946666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	5	455	1	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	8.85e-50	1	458	1	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	1.46e-29	44	390	33	347	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	2.32e-29	6	505	2	492	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	7.63e-22	34	390	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
QCD40429.1	4.26e-249	1	567	6	573
QCP71534.1	4.26e-249	1	567	6	573
QCD41202.1	4.16e-246	1	554	2	556
QCD35086.1	8.23e-244	2	558	3	560
QQR07864.1	2.41e-235	3	558	4	560

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	2.67e-17	33	388	26	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	7.19e-16	6	388	7	291	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]
5M99_A	1.27e-13	5	506	6	424	FunctionalCharacterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization [Thermotoga petrophila RKU-1]
5M99_B	1.27e-13	5	506	5	423	FunctionalCharacterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization [Thermotoga petrophila RKU-1]
4E2O_A	4.45e-13	34	409	42	345	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14899	9.48e-14	6	458	36	425	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
P21567	2.08e-12	6	414	41	388	Alpha-amylase OS=Saccharomycopsis fibuligera OX=4944 GN=ALP1 PE=3 SV=1
P14014	6.29e-11	34	455	86	465	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA PE=3 SV=1
P31797	8.25e-11	47	454	94	466	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P05618	8.26e-11	47	444	93	450	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1011) OX=1410 GN=cgt PE=1 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
1.000090	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003164_02202.