CAZyme Information: MGYG000002168_01051

Basic Information

• Species: Prevotella sp900556825
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900556825
• CAZyme ID: MGYG000002168_01051
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
689	MGYG000002168_21|CGC1	75393.8	5.8093

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002168	3553249	MAG	Denmark	Europe

• Gene Location: Start: 301; End: 2370 Strand: +

Full Sequence      

MKKIYTFLLLLLAIPMTLMAGDGWPKNYSGVMLQGFYWDSYDHTSWAQLTNKASDLKGYI
DLVWIPQSAKAVGSPSMGYDPLYWFSHYDSSFGTEAELRTLISTFKSAGIGTIADVVINH
RGNISNWVDFPKETYKGTTYQLLSMDICADDDDGATKTWADANGYTLSSNKDTGEGWSGM
RDLDHNSSNVQANVKAYLNMLLNDFGYAGFRYDMTKGYSGSFTGLYNSNANPTYSVGEYW
DGNATTVEAWLNATKVNGVIQSAAFDFPFRYTVRDAINGTTDGTVGSSSDWTKLSNASLA
ATTAYQQYAVTFVENHDTEYRSSTSPQDPIRKDTLAANAFLLAMPGTPCIFYKHWATYEQ
ELKSMIDARKIAGITNQSSFTNMRSNTKYYANKVSGSKADLIVLVGDDVSAYTPSSSSYT
QILSGYHYKYFLGNTAETAWADKASGSYTGSSLSVKLTAVSQTAGAQLVYTTDGSTPTAS
SKTATSGNSITLPVGTTTLTVGLLINGTVSGIISRTYTVAEPVAFTPYTITVCVNGDQVG
WTNYINFWSWGGDDSHAPQNSSWPGDKVTTSKTVNGKTWFYQTYTINSADDYVSFVFSTA
SGSPQTVDVTKIKTDKYFEISTEQSGTKYQVMDVTPTTGIHAVTKDEPEHTHVYSIDGRL
IRENVKTADALNGLPKGIYIVNKKKVIVR

Enzyme Prediction     

No EC number prediction in MGYG000002168_01051.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	60	355	1.6e-48	0.9653979238754326

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11314	AmyAc_arch_bac_plant_AmyA	5.18e-117	31	379	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.
PLN02361	PLN02361	3.12e-44	26	428	8	396	alpha-amylase
PRK09441	PRK09441	1.40e-42	30	370	4	392	cytoplasmic alpha-amylase; Reviewed
PLN00196	PLN00196	9.85e-39	7	414	10	410	alpha-amylase; Provisional
cd11318	AmyAc_bac_fung_AmyA	2.44e-36	30	370	2	390	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
QUB75387.1	1.14e-249	1	689	1	675
QKH89892.1	2.46e-249	22	689	3	658
QUB62461.1	2.29e-247	22	689	3	658
QUB80123.1	2.93e-247	1	689	1	675
QUB87660.1	5.87e-245	22	689	3	657

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AMY_A	5.53e-35	31	396	2	368	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]
2QPS_A	7.16e-31	31	415	3	388	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
1HT6_A	7.16e-31	31	415	3	388	CrystalStructure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 [Hordeum vulgare],1P6W_A Crystal structure of barley alpha-amylase isozyme 1 (AMY1) in complex with the substrate analogue, methyl 4I,4II,4III-tri-thiomaltotetraoside (thio-DP4) [Hordeum vulgare],1RPK_A Crystal structure of barley alpha-amylase isozyme 1 (amy1) in complex with acarbose [Hordeum vulgare]
3BSG_A	8.25e-31	31	415	3	388	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSH_A	8.25e-31	31	415	3	388	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	4.60e-34	31	396	26	392	Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
P08117	1.67e-33	31	396	27	375	Alpha-amylase AMY3 OS=Triticum aestivum OX=4565 GN=AMY1.1 PE=2 SV=1
P27932	8.76e-33	31	394	30	392	Alpha-amylase isozyme 3A OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.2 PE=2 SV=2
P04747	3.94e-32	31	367	26	359	Alpha-amylase type B isozyme (Fragment) OS=Hordeum vulgare OX=4513 GN=AMY1.3 PE=2 SV=1
Q8LFG1	8.73e-32	31	428	27	408	Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 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
0.000763	0.998009	0.000475	0.000238	0.000249	0.000251

TMHMM  Annotations     

start	end
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