CAZyme Information: MGYG000001056_01358

Basic Information

• Species: Prevotella sp900556395
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900556395
• CAZyme ID: MGYG000001056_01358
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
651	MGYG000001056_115|CGC2	72935.37	5.4354

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001056	3020119	MAG	Spain	Europe

• Gene Location: Start: 35553; End: 37508 Strand: -

Full Sequence      

MKKLYFTLLAAMALTLGACSSSNDPDIPPTPTPTPEPEPEPGPGPSLTSQGWPINYGGVM
LQGFSWDSYNDSQWKILANQTDDMKGYIDLVWLPQSGKCAETVQVMGYKPYYYFNQNSSF
GTETELRNLITKFKANGIGAIADVVINHRNTEGWFTFPAETYKGVTYQMLSTDICKNDDQ
GKTATQAATDGVSLSNNNDEGTDFDDCRDLDHKSANVQKIMKAYVDYLKNDLGYIGFRYD
MVKGFDGIHVADYNDAVGVEYSVGEYWDGNDKIESWINKTNKKSAAFDFQFRYNVRDAVN
GTTNGKLGSSSDWSKLYSSNNLMHDASYRRYAVTFVENHDTQYRSADSQNDPLRKDTLAA
NAYLLAMPGTPCIFQIHWNEYKPELKEMIAARKYAGITNMSNYVNRTSKKTLYVNEVTGS
NHKLLVAVGDEASNYAGETGYTKIFKGHHFSYFLSNDAETTWTSMPSGTYEEGFKTTLTA
VSQTEGAKLVYTLDGSTPTAKSTTVESGKEISINGTCTLKVGLLVNGEVRNIATHQYTIE
KFKAYKFMVYVNVDAVKWNPLYCYSWKKEASVEWPGEKMTETKTIGGKTWYYKEFSIDKA
SELVNVIFNNGTGKPQTIDITGLTNTAYFEIETTKEGKNYKVKNVTSEYDK

Enzyme Prediction     

No EC number prediction in MGYG000001056_01358.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	88	375	2.6e-49	0.9550173010380623

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11314	AmyAc_arch_bac_plant_AmyA	1.03e-115	59	402	1	301	Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 AmyA from bacteria, archaea, water fleas, and plants. 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.
PRK09441	PRK09441	4.25e-50	57	394	3	393	cytoplasmic alpha-amylase; Reviewed
PLN02361	PLN02361	9.66e-40	59	430	13	377	alpha-amylase
PLN02784	PLN02784	1.59e-38	59	429	504	866	alpha-amylase
cd11318	AmyAc_bac_fung_AmyA	2.04e-38	58	394	2	391	Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNT66936.1	1.91e-291	1	647	1	622
BCS84551.1	1.00e-233	49	647	19	609
QUB70315.1	5.06e-227	50	647	23	625
QUB90758.1	7.17e-227	50	647	23	625
QUI94094.1	2.04e-226	50	647	23	625

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AMY_A	1.27e-35	59	429	2	375	CrystalAnd Molecular Structure Of Barley Alpha-Amylase [Hordeum vulgare],1AVA_A Amy2BASI PROTEIN-Protein Complex From Barley Seed [Hordeum vulgare],1AVA_B Amy2BASI PROTEIN-Protein Complex From Barley Seed [Hordeum vulgare],1BG9_A Barley Alpha-Amylase With Substrate Analogue Acarbose [Hordeum vulgare]
3WN6_A	1.32e-33	59	429	3	376	Crystalstructure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group],3WN6_B Crystal structure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group],3WN6_C Crystal structure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group],3WN6_D Crystal structure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group]
2QPS_A	1.78e-31	59	432	3	380	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSH_A	2.06e-31	59	461	3	410	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSG_A	3.77e-31	59	461	3	410	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P04063	3.08e-35	57	429	24	399	Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
Q8VZ56	1.16e-33	59	414	27	383	Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1
P17654	3.47e-33	57	429	31	406	Alpha-amylase OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.1 PE=1 SV=2
P04747	6.92e-33	57	392	24	365	Alpha-amylase type B isozyme (Fragment) OS=Hordeum vulgare OX=4513 GN=AMY1.3 PE=2 SV=1
P08117	2.10e-32	59	429	27	382	Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000038	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001056_01358.