CAZyme Information: MGYG000003353_00278

Basic Information

• Species: Prevotella corporis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella corporis
• CAZyme ID: MGYG000003353_00278
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
671	MGYG000003353_54|CGC2	74552.57	7.1339

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003353	2741974	MAG	China	Asia

• Gene Location: Start: 22788; End: 24803 Strand: -

Full Sequence      

MKKIFTLLTLCCIALSSLAQGWQDNYKGVMLQGFYWDSFDDTKWTNLEAQTNDIADFFDL
VWIPQSAKPSHNPSMGYDPLYWFSDYNSSFGTEKELLSLIDTWKKNGIGTIADIVINHRG
NVSNWFDFPTETYEGVTYTMGATDIVKDDDKGKTQVEATKQGVSVSQNNDTGEGWDGMRD
LDHHSPNVQKTVKAYLNMLINKFGYSGFRYDMVKGYAGSFTGLYNTATQPQFSVGEYFDS
NLAKVKNWIESTRTGGVITSAAFDFPLRYAIRDAVNNGNWAALDGQGLAKLPDYARYAVT
FVENHDTEDRGSGNTQDPIRNNISAANAYIMAMPGTPCVFLKHWQSCKKDIKNMITVRKL
LGISNRSTATKLVSGNDFYAMVTKGDMGNLLTVVGPAATFATQSKWIKITGGENWAYYAD
KNTSSFAWADLPSGSYDGVQSVTLRAVTGNPNAKIVYTIDGSDPKASSSMTENESKITIP
EGKATTLKVGLLINGTVTGISTRHYDIVDFQPYNISVYVNADNADDTWAEAKTSSPTPSI
NYYYWGSATSSPWPGNAVTTTTEIGGKRYFVKQFRINSSADAINFVFNMGMNKSQTVDVM
NIRQDTFIDISSQKDDWKYKVNTTTAIRGIECEKTGNKNESSYYYTLSGQRLKKPVQPGI
YIHKGKKIIIK

Enzyme Prediction     

No EC number prediction in MGYG000003353_00278.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	58	340	9.6e-54	0.9688581314878892

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11314	AmyAc_arch_bac_plant_AmyA	1.53e-122	29	367	1	300	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.
PLN02361	PLN02361	2.37e-50	25	382	9	366	alpha-amylase
PRK09441	PRK09441	3.65e-45	28	359	4	392	cytoplasmic alpha-amylase; Reviewed
PLN00196	PLN00196	2.08e-35	29	379	26	387	alpha-amylase; Provisional
PLN02784	PLN02784	2.96e-35	29	382	504	856	alpha-amylase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUB52626.1	1.80e-311	1	671	1	672
QUB54439.1	2.96e-310	1	671	1	672
QUB49498.1	5.96e-310	1	671	1	672
ATV54979.1	2.15e-305	1	671	1	672
ATV40839.1	3.05e-305	1	671	1	672

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WN6_A	4.35e-34	29	396	3	377	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]
1AMY_A	1.07e-33	29	391	2	384	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]
2QPU_A	7.93e-32	29	396	3	378	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare],2QPU_B Chain B, Alpha-amylase type A isozyme [Hordeum vulgare],2QPU_C Chain C, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSH_A	1.24e-31	29	379	3	364	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
2QPS_A	1.46e-31	29	379	3	364	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P17859	3.13e-43	5	391	4	404	Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1
Q8LFG1	1.32e-39	27	418	25	411	Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1
Q8VZ56	5.61e-39	29	379	27	382	Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 PE=1 SV=1
P08117	1.18e-38	7	379	12	369	Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1
P27934	6.42e-38	8	396	6	399	Alpha-amylase isozyme 3E OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.4 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000252	0.999006	0.000215	0.000166	0.000168	0.000157

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003353_00278.