CAZyme Information: MGYG000000392_00850

Basic Information

• Species: Ruminococcus_E sp003521625
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp003521625
• CAZyme ID: MGYG000000392_00850
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
879		94415.55	4.734

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000392	2042501	MAG	Sweden	Europe

• Gene Location: Start: 237256; End: 239895 Strand: +

Full Sequence      

MSKKIMSVILALCMTLSCLTAAGIVAEARTTETAEVSAQATSVETGADYGLVDDVQDGQI
LQCWNWSYNGIKANMQKIAEQGFSAIQTSPIQTIKETTQNRQMSGSWWVFYQPSDFKIDT
SSQNALGTKSDFKSMCDEAHKYGVKVIVDAVLNHMANNGDNTLSPTIPSDIRNDSSCWHS
ITTNTSNWNSRWDITHNCMGGLPDLNTGNSKIQNYEIAFLKECIDAGADGFRFDGAKHIE
VPNDNENASSNFWSNVLGAATSYAKSSRGFTPYYYGEILDSTGGGQSIVNQYTNYMSVTC
NTVSDNIRSQVNSGNASGAKRKDFCYNDGSQPAASKAVLWNESHDTYANGSSRGQSDTTL
KKTWALVGSRAQACGMYLARPSSYSNQIGTASVTAWGDVEVKAVNQFKNYFVGKTEYPSS
EGSIAYNERGTEGVVLVNCGGSSTSVSVTAHKMAAGTYTDQITGNTFTVSNGKISGKIGS
TGVAVVYNAKPAGPSASVTPGSQSYNTDTLTLTLNYKNATSGQYSIDGGSYQSFTDGKTI
TIGSGLAYGTKTTVSVKATDGTTTSDIQTYTYTKVDPSLVQKVYFDNSSYNWSSVYAYIY
ADSSTNNGAWPGAQMTKDSATGYYVIEVPEELSNGYVILTESKDATSNRYPADGETGMAL
NGKTMIMRANHSWEEYTVTPATTAAPTTQPTTAVPTTVPVTTVPADKVLIGDTNIDGKIT
ISDATEIQYHISEYSTLTGDNAIAADTDKNGTINIKDATVIQYYLVGLTESAGHCGEYTG
GETPTTQPTTAPSGDYVYYYNSNGWSSVNAYYWSDDNTSLTKWPGVDMESVGNNVYRTKY
PSAATYIIFSNNGSNQTSTITLSGANKIYKNGSWSTYNG

Enzyme Prediction     

No EC number prediction in MGYG000000392_00850.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	66	351	6.5e-91	0.9924812030075187

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	8.81e-111	57	417	1	351	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	3.20e-35	60	358	4	250	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.
cd11320	AmyAc_AmyMalt_CGTase_like	3.20e-18	70	240	48	219	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.
smart00642	Aamy	1.17e-17	59	160	1	100	Alpha-amylase domain.
COG0366	AmyA	1.47e-17	66	252	26	216	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT06294.1	6.06e-268	3	738	5	739
AET60999.1	1.69e-115	48	666	45	646
APB71173.2	2.01e-115	48	666	53	654
ASR47410.1	8.60e-115	45	666	42	646
AWB44629.1	1.57e-114	23	666	23	650

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	1.40e-83	55	487	3	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UA7_A	1.43e-82	55	487	3	420	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	3.02e-82	55	487	6	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1CLV_A	1.16e-16	60	295	13	239	YELLOWMEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR [Tenebrio molitor],1JAE_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE [Tenebrio molitor],1TMQ_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR [Tenebrio molitor]
1VIW_A	2.05e-16	60	295	13	239	TENEBRIOMOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	8.03e-100	55	662	47	646	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	1.97e-68	51	513	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	1.18e-58	47	628	135	752	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P29750	4.50e-20	60	239	42	224	Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam PE=1 SV=1
P83833	3.18e-17	60	239	31	209	Alpha-amylase A OS=Drosophila yakuba OX=7245 GN=Amy-p PE=3 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
0.001017	0.902829	0.094835	0.000738	0.000297	0.000247

TMHMM  Annotations     

start	end
7	26