CAZyme Information: MGYG000001738_01756

Basic Information

• Species: Duncaniella sp001701225
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella sp001701225
• CAZyme ID: MGYG000001738_01756
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
567	MGYG000001738_19|CGC2	64346.64	5.4368

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001738	3129928	MAG	Sweden	Europe

• Gene Location: Start: 19488; End: 21191 Strand: +

Full Sequence      

MDRKPIIYQLFPRLFTNTNTACIPNGTLAQNGVGKMNQITDTVLQGIKQLGVTHIWYTGL
IEHATKTDYTAEGIVPADNPYVVKGEAGSPYAIKDYYDIDPDLAESVPDRMAEFEALVAR
THDNGMEVVIDFVPNHTARRYHSDVAPAGIEDFGAHDDSNMFFSPNNNYYYITRQLFAPS
IDLGTGKQAYIEFPAKATGDDCFTAFPSSGNWYETVKLNYGRDPMNGSGHYSPIPDTWFK
MLNILRYWASKGVDAFRCDMAHMVPIEFWQWAIPNVKDRYPHIKFIAEIYDVGLYRDFIN
VAGFDYLYDKVNLYDTLRGIQTANHSAATITSCWQAVDGIQPHMLNFLENHDEQRFGSKF
YAGDPAKVIPSLVVSSMISTGPMMIYMGQELGEQATDSEGFSGYDGRTTIFDYWSVGTLR
RWYNEGNPDGSQLTPRERWLRAKYATILRLCNTEKAIAHGRFYDLMYVNYQNPTLNPHRQ
YVFMRSYDGVTLFIAANFASESCDLSVNIPRHALEMLNIPEGNVMSRELLTGETDVKTIS
ATEPFRTMIPPYDAVVWKIIHKNIKQA

Enzyme Prediction     

No EC number prediction in MGYG000001738_01756.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	31	397	7.8e-166	0.9973333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	5	457	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	2.96e-50	3	393	3	296	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	3.88e-34	35	392	24	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	3.10e-28	6	507	2	492	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.87e-24	6	393	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
QCD41202.1	0.0	1	566	2	566
QCD40429.1	0.0	1	566	6	570
QCP71534.1	0.0	1	566	6	570
QCD35086.1	6.58e-305	4	564	5	564
QQR07864.1	9.74e-290	2	566	3	566

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	1.50e-18	84	390	61	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	355	7	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]
1CYG_A	7.42e-14	6	390	13	359	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
1UKS_A	4.85e-12	6	440	16	414	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1UKS_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]
1V3K_A	1.47e-11	6	440	16	414	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3K_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3M_A Chain A, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3M_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P31797	4.20e-13	6	390	44	390	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P14014	1.57e-11	6	440	50	448	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA PE=3 SV=1
P08137	1.61e-11	6	440	44	443	Alpha-amylase OS=Niallia circulans OX=1397 PE=3 SV=1
P09121	1.09e-10	6	440	43	441	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 38-2) OX=1412 GN=cgt PE=1 SV=2
P14899	1.43e-10	3	396	33	357	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC 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
0.999721	0.000327	0.000002	0.000001	0.000000	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001738_01756.