CAZyme Information: MGYG000001557_00241

Basic Information

• Species: F0040 sp900095835
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; F0040; F0040 sp900095835
• CAZyme ID: MGYG000001557_00241
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
566		64038.99	5.0866

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001557	2753132	Isolate	not provided	not provided

• Gene Location: Start: 256699; End: 258399 Strand: -

Full Sequence      

MNIYQVFTRLYGACKPAKNLPNGTIADNGVAKFNEFTADTLQRIKDYGFTHVWFTGVLEH
ATKTDYTRYGIHLDHPWIVKGRAGSPYAIKDYFDVDPDLAEDVPNRMAEFEALLERTHKT
GLKFVIDFVPNHVARSYHSDVAPKGFEDLGVGDDEELAFTPRNNFYYCWGEPLHTENFVE
AEKGGIPYLEHPAKATGNDVFHAWPNRNDWYETVKLNYGVDYNGGGAQHFAPIPSTWQKM
TDILLFWASKGVDAFRCDMAEMVPVAFWHYAIAQVKAKYDVQFIAEVYNPNEYRNYIHHG
GFDYLYDKVGLYDTLRAVICQQTSAAAITNAWQNTDDIKKHMLYFLENHDEQRIASDFFC
GDAQKAIPGLVVAACMGNNPLMIYAGQEIGEKGMDAEGFSGKDGRTTIFDYWSVPSLHKL
SSISPSLKSTKSPNQVLTGEELALYQDYQRILRLRNENKSLSEGLFYDLMYVNYDGAEGF
DCHRQYAFLRKTEGELLFCVANFSDTYIECGIRIPAHAFDFLSIPSGEYSAVDLISGEES
NISLAPDACTQIKVRANNAILLSVKF

Enzyme Prediction     

No EC number prediction in MGYG000001557_00241.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	28	395	8.7e-176	0.9973333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	1	461	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	3.46e-54	1	464	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	1.30e-39	3	392	3	349	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	4.47e-25	2	506	2	486	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	8.26e-21	3	376	2	241	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
QRQ47597.1	3.12e-239	3	565	9	564
QUT46856.1	3.12e-239	3	565	9	564
QFQ12053.1	7.94e-239	3	562	6	550
BCA50275.1	5.11e-238	1	566	7	565
QMW87802.1	2.93e-237	1	566	7	565

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	6.32e-18	3	388	15	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	3.97e-14	3	355	8	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]
4AEF_A	1.24e-13	87	518	270	631	TheCrystal Structure Of Thermostable Amylase From The Pyrococcus [Pyrococcus furiosus],4AEF_B The Crystal Structure Of Thermostable Amylase From The Pyrococcus [Pyrococcus furiosus]
4E2O_A	9.48e-11	41	460	51	404	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6YUP_A	2.35e-10	87	263	175	319	ChainA, Neutral and basic amino acid transport protein rBAT [Homo sapiens],6YUP_C Chain C, Neutral and basic amino acid transport protein rBAT [Homo sapiens],6YUZ_A Chain A, Neutral and basic amino acid transport protein rBAT [Homo sapiens],6YUZ_C Chain C, Neutral and basic amino acid transport protein rBAT [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20845	1.26e-12	87	512	101	488	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
Q07837	1.29e-09	87	263	175	319	Neutral and basic amino acid transport protein rBAT OS=Homo sapiens OX=9606 GN=SLC3A1 PE=1 SV=2
P07190	3.50e-09	28	267	42	227	Maltase A1 OS=Drosophila melanogaster OX=7227 GN=Mal-A1 PE=2 SV=2
O16098	3.72e-09	87	258	140	280	Maltase 1 OS=Drosophila virilis OX=7244 GN=Mal-B1 PE=3 SV=2
Q91WV7	5.14e-09	87	263	174	318	Neutral and basic amino acid transport protein rBAT OS=Mus musculus OX=10090 GN=Slc3a1 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
1.000041	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001557_00241.