CAZyme Information: MGYG000001806_01937

Basic Information

• Species: Prevotella sp900553965
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900553965
• CAZyme ID: MGYG000001806_01937
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
664	MGYG000001806_81|CGC1	74207.74	6.7066

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001806	3097082	MAG	Denmark	Europe

• Gene Location: Start: 8490; End: 10484 Strand: +

Full Sequence      

MRRFYSLIVALFATISIQAQGWPAQYGGVMLQGFSWDSYDYSQWSILESQAADMKGFIDF
VWVPQSGKCLETTQVMGYMPYCYFQHDSSFGTEAELRSMIRTFKENGIRTMADVVVNHHQ
TDGWFDFPAETYKGVTYQFKSTDICRNDDGGATLKQANAQGVSLSPNNDEGEDFSGGRDL
DHKSENVQRIIKAYVKYLKDDLGYEGFRYDMVKGFDGSHVADYNDAAGIGYSVGEHWSGV
SETSSWIKATGYKSAAFDFQFHYAMTDAIKQNNWQQLNNHKTLMHDAAFRRYAVTFVENH
DIQDRGVPDGQYNTKDPINEPYILAANAYLLAMPGTPCIFQPHWRAYEQELKSMIEARKL
AGITNTSDFGSYLSNTAYCQTFAKGEGNKRLMVAVGDETKFSVPNNYTRILSGSHYAYFL
TKNSETAWADKPSGTYDGAFDVTLTAVSEDAGAKLVYTLDGTAPTAGSQQVSSGTTVRID
KACTLKVALLIGGKVTGMTTKEYAIKTFEPYSFKVYVCTDKVSWKNINFYSWGTNSKNSS
AAWPGDRITATETVNGRTWYVKEFYIDSKNDLVNFVFSTGTGSPQTVDKTGVSKTAYFEI
STTMSNGKHTISDVTKDMTSGIHAPAIGTSRDDSGWYDISGRRYDKRPAYRGLYIHQGKK
HVIK

Enzyme Prediction     

No EC number prediction in MGYG000001806_01937.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	58	340	1.8e-47	0.9688581314878892

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11314	AmyAc_arch_bac_plant_AmyA	1.30e-108	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.
PRK09441	PRK09441	4.14e-42	27	359	3	392	cytoplasmic alpha-amylase; Reviewed
PLN02361	PLN02361	2.72e-40	29	359	13	343	alpha-amylase
PLN02784	PLN02784	1.24e-36	29	363	504	837	alpha-amylase
cd11318	AmyAc_bac_fung_AmyA	1.55e-33	28	360	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	2.37e-271	1	664	1	672
QUB75387.1	1.99e-246	1	664	1	675
QUB80123.1	4.42e-240	1	664	1	675
QUB62461.1	6.98e-240	19	664	2	658
AKU69270.1	2.44e-239	1	664	1	674

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AMY_A	4.59e-31	29	367	2	350	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]
3BSH_A	7.39e-31	29	427	3	409	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3BSG_A	1.35e-30	29	427	3	409	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
1HT6_A	1.59e-30	29	367	3	352	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]
2QPS_A	1.59e-30	29	367	3	352	ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8LFG1	1.68e-34	29	417	27	409	Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1
P27933	2.48e-34	1	417	1	421	Alpha-amylase isozyme 3D OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.3 PE=2 SV=2
P17859	3.57e-34	29	417	25	418	Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1
P27932	9.01e-34	29	416	30	423	Alpha-amylase isozyme 3A OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.2 PE=2 SV=2
P27939	2.46e-32	29	363	28	370	Alpha-amylase isozyme 3C OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.7 PE=2 SV=2

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
0.000384	0.998793	0.000168	0.000225	0.000202	0.000187

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001806_01937.