CAZyme Information: MGYG000001036_00156

Basic Information

• Species: CAG-1031 sp900752535
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-1031; CAG-1031 sp900752535
• CAZyme ID: MGYG000001036_00156
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
578		65686.27	5.8122

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001036	3018511	MAG	Sweden	Europe

• Gene Location: Start: 2860; End: 4596 Strand: +

Full Sequence      

MKPVIYQLLPRLFTNINEDLRPNGTVAENGSGKLNDINDRVLSSIKDLGVTHVWYTGVIE
HATKSDYTAHGIRRDNPHIVKGQAGSPYAIKDYYDINPDLAEDVDNRMAEFEALVERTHR
AGLKVIIDFVPNHLARQYFSDQLPKGVDNPGTHDDTSLYFGRDNNFYYIPRQLFAPHMDL
GIGQDAYIEFPAKASGNDCFNAFPGPNDWYDTVKLNYGVDYGDGSRHFDPVPDTWFKMLH
ILRFWASKGVDGFRCDMVHMVPLEFWEWAVIEVKRHHPGIIFIAEIYDVGLYRPFIDRGG
FDYLYDKVNLYDTLRGIMTSNFSAATLTNSWQTVDGIGPHMLNFLENHDEQRFGSRFYAG
NPALVTPSLVVSAMLSTGPMMIYMAQELGEQALDAEGFSGDDGRTTIFDYWSLATLRRWF
SDIEGLTGLSDRERWLRDIYRRVLRLCNSEKAISDGAFFDLMYVNYDNPTLNPHRQFVFM
RSKDNEVLLIAVNFGDYDAHLKINIPQHAFETLAIEPAANAAAVELLSETTAIRSLSPAV
PFDTTVPPFGAVVWKIVTPERSRQKKAVSRRVIKAKKS

Enzyme Prediction     

No EC number prediction in MGYG000001036_00156.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	29	393	2.3e-167	0.9946666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	3	453	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	9.10e-53	4	456	6	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	1.55e-40	33	357	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	2.83e-31	4	506	2	493	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.92e-29	4	390	1	259	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	4.96e-298	2	556	5	559
QCD40429.1	5.71e-288	2	556	9	563
QCP71534.1	5.71e-288	2	556	9	563
QCD41202.1	2.41e-286	2	571	5	570
QQR07864.1	8.92e-284	2	556	5	559

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	1.14e-20	42	387	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	4.20e-16	39	352	28	260	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]
4CGT_A	6.72e-16	4	440	16	413	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]
3CGT_A	8.96e-16	4	440	16	419	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans],8CGT_A Chain A, PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) [Niallia circulans],9CGT_A Chain A, PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) [Niallia circulans]
1WZA_A	1.02e-15	33	456	32	410	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14014	2.93e-15	4	440	50	453	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA PE=3 SV=1
P31797	8.86e-15	4	387	44	390	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P30920	8.93e-15	4	440	50	453	Cyclomaltodextrin glucanotransferase OS=Niallia circulans OX=1397 PE=1 SV=1
P31747	6.28e-14	4	440	50	453	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 6.6.3) OX=29335 GN=cgt PE=3 SV=1
P31746	4.34e-13	2	440	39	441	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1-1) OX=29334 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
1.000057	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001036_00156.