CAZyme Information: MGYG000004629_01502

Basic Information

• Species: Prevotella intermedia
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella intermedia
• CAZyme ID: MGYG000004629_01502
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
564	MGYG000004629_28|CGC1	64125.91	4.8912

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004629	2382499	MAG	Germany	Europe

• Gene Location: Start: 14789; End: 16483 Strand: -

Full Sequence      

MKLVIYQVFTRTFGNKNNNRKPNGTLAENGVGKMNDFDVATLQRIKSFGVNTIWYTGVIR
HATCTDYSAFGIPRQTPRVVKGKAGSPYAITDYYDIDPDIADNVAERMSEFEDLVKRTHK
EGLKVIIDFVPNHVAREYKSICKPKGVKDLGETDDTGKHFDANNNFYYCPNEPLDTSAIP
LPNGIEADNSNEMVAEYTETVARCTGNDRFDAHPRANDWYETVKLNYGVDYCDWGGRSTH
FEPIPDTWHKMTDILLFWAAKGVDGFRCDMAEMVPHEFWKYATEKVKAQYPHIVFIGEVY
DPNQYRTYVAAGFDYLYDKVGMYDCLRDVMCGHRSASNISQQWQATDDIHEHILYFLENH
DEQRIASDFFCGNMQKGIPALIVSALFQRNPVMIYAGQEFGERGMDSEGFSGVDGRSTIF
DYWSVDAIRKGFFERSELSAEQLQLEKNYRTILNICNSEKAVSEGKTFDLMYANEANEGF
DSNRLFAFLRSFGNTTLLVVANFGEAEAHVRVNIPAHAFDYMELTEGKKDMVDLLSGDQQ
TAILQQDSPVEMVVAGLSGRIYKF

Enzyme Prediction     

No EC number prediction in MGYG000004629_01502.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	29	406	3.7e-180	0.9973333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	3	462	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	2.29e-56	4	402	6	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	1.13e-36	42	369	33	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	1.79e-26	4	512	2	492	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	3.88e-24	4	396	1	253	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
AWX07627.1	0.0	1	564	1	564
ATV28043.1	0.0	1	564	1	564
ATV31375.1	0.0	1	564	1	564
ATV33586.1	0.0	1	564	1	564
ATV40006.1	0.0	1	564	1	564

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	8.36e-18	4	400	14	314	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	1.67e-17	42	366	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]
7JJT_A	5.66e-14	79	508	82	475	ChainA, Alpha-amylase [Ruminococcus bromii]
1SMA_A	2.28e-11	57	542	177	566	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
6YUP_A	3.35e-11	5	327	123	362	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
L8B068	1.47e-15	4	550	249	646	Alpha-amylase MalA OS=Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1) OX=1227453 GN=malA PE=1 SV=1
P14899	1.65e-13	4	545	36	497	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
P20845	1.25e-12	88	512	101	488	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
A0A7U9P668	9.44e-11	57	542	177	566	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1
Q07837	1.83e-10	5	327	123	362	Neutral and basic amino acid transport protein rBAT OS=Homo sapiens OX=9606 GN=SLC3A1 PE=1 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
0.998183	0.001770	0.000059	0.000006	0.000003	0.000011

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004629_01502.