CAZyme Information: MGYG000001927_01530

Basic Information

• Species: Prevotella sp900547005
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900547005
• CAZyme ID: MGYG000001927_01530
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1223	MGYG000001927_23|CGC1	130697.34	4.9332

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001927	2803818	MAG	Denmark	Europe

• Gene Location: Start: 26353; End: 30024 Strand: +

Full Sequence      

MNQSLLRTSKKVLGLLLMLAITLASQVNAQNLYGIPSGIQEGNILHCFNWKISDVKAELP
NIAAAGFGSVQLSPLQRNSAVGSTWADIYRPYDFKFIASGLGTKEDLTSLCAEAEKYGIK
IIVDVVANHVDGHGAGDHSLYHDPWWNSNNRLRWNGDCNYGDRNSITHNQMGGGSGYPDV
NSEDPEVANRAKAYIEELKACGVKGIRWDAAKHIALPSEGCQFWATVTSVPGMYHYGEIL
DNPGGGNGDNLMKEYTNYMSVTDNGYGNGARNNGGVPSSNAGWAGGTLFKADKVVYWGES
HDTYANYNGESKNVSQDVIDRAYAIVGCRDGATALYFSRPAAKNFNDIKVGAKGSTNFTG
KQVAEVNKFRNAMNGKKEYYTQNNGVASLTREGGGAVIVNRNGSGNVSIANGGGYCPAGT
YTDRVSGGTFTVTSTTISGNVGSSGIAVIYGEVVQKPSVTLSPNGGSFTETQTVTATLNN
ATSGWYKIGDGAQQSFTGTTTFTIGSNMAVGESVTVSWSATGEEGTKTGQATFTKRDPSA
IVTVYYNNPGNWSSVNCYIYLPDTDPAKANGTWPGASMAKDASTGLWYYEVPEGLTTSAK
VIFSGGGSQYPADVAGQSCGLDLNGKSMICKNNSSWTEYNGDEPGPGPQPGSVTITGDYN
LAYSGTKEKVYYWKVSSPDWPGVKMETATGSDGKTYKVFKVPEGTTGIIFNTNGDADKTK
DLTYTGEYVMDDNGATSTKVTFSSDPQPTKPIVSASPANGSFTESISVTLSVNPAATIYY
TTDGTTPSTSSQKYSSALTFTETTTLKAFGVTSDGTSGDVKTFTYTKSSGPGPQPQPGDN
LITDYYKVNPNGQVGTNRTVNMSFNGQKSTTALNNWTEADLVAQGVARDICQAFKGVHER
PIVDSYALYAAYDNENLYLGVQYVYTVWDIAGEGKQPGESKPYNMDGKLSFAFDLDPDKS
AKGITNENTSIWQDNIYTTFDNGADAWWFGSTKPGVGTPGYFVPNASGICDYKDPASCKK
SEVTYGYADGVLPSITAIYGQDDFSYDPELLKGNNGFTDLSGEIDNSAHTFYEFKFPLSM
MGITADHIRNNGIGVMVVDYYGASAHSSLPYDPSFYDNVFEAYSKDDSSSKEKEDQDVVT
YAMARIGKLKATGISNIVAGNNANGIKVRVAGGRLYIESDKAQDVTISTVSGMTKVQKVN
AGVNVIDGLAHGIYIINRTKVVL

Enzyme Prediction     

No EC number prediction in MGYG000001927_01530.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	50	307	1.8e-52	0.9887218045112782
CBM74	846	1145	7.2e-49	0.9967948717948718
CBM26	543	612	1.8e-18	0.8933333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	1.38e-94	41	380	1	352	Alpha amylase catalytic domain found in 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, Proteobacteria, Actinobacteria, and Cyanobacteria. 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.
cd11317	AmyAc_bac_euk_AmyA	1.05e-20	44	303	4	238	Alpha amylase catalytic domain found in bacterial and eukaryotic 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 proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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.
pfam13290	CHB_HEX_C_1	2.45e-18	757	822	1	67	Chitobiase/beta-hexosaminidase C-terminal domain.
cd11319	AmyAc_euk_AmyA	5.87e-16	62	263	52	251	Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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.
cd11320	AmyAc_AmyMalt_CGTase_like	1.70e-15	57	272	51	276	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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
QNT67433.1	4.72e-149	15	711	10	722
CDM67953.1	9.17e-131	29	1148	37	1085
QUB83913.1	5.46e-119	39	450	31	434
QFJ55411.1	1.04e-111	33	449	46	464
AWX95531.1	7.62e-109	39	1147	29	1061

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UA7_A	3.24e-57	39	450	3	420	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	1.18e-56	39	450	6	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
3DC0_A	1.49e-56	39	450	3	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1G94_A	5.91e-13	45	309	6	271	CRYSTALSTRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]
1JD9_A	6.04e-13	45	309	6	271	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	2.52e-80	24	611	33	633	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	4.93e-47	35	475	47	488	Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2
P30269	2.79e-35	39	722	145	888	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P22630	1.88e-20	44	376	24	385	Alpha-amylase OS=Aeromonas hydrophila OX=644 PE=3 SV=1
P53354	7.11e-16	44	356	271	607	Alpha-amylase I OS=Aedes aegypti OX=7159 GN=AMY1 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
0.000224	0.999181	0.000151	0.000149	0.000136	0.000127

TMHMM  Annotations     

start	end
12	29