CAZyme Information: MGYG000003990_01826

Basic Information

• Species: Ruminococcus_E sp900314705
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp900314705
• CAZyme ID: MGYG000003990_01826
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
896		96683.69	5.1526

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003990	2132910	MAG	United Kingdom	Europe

• Gene Location: Start: 1404; End: 4094 Strand: +

Full Sequence      

MKCKKKFVSFVLSLCMAVTATSIPVVSAVSTDKSASKASTTTVSTSANAYGLADNIQDGQ
ILQCFNWSFDNIKKNMKTIAEQGFTAVQTSPIQVAKESTTGKTAKGSWWVLYQPVDFAIE
TNAHGTSALGTASQFKAMCDEAHKYGVKVVVDAVLNHMGNKSKNDLSPCIPDEIRNNSSL
WHDISKNSWYASRHDITQYCMDGIPDLNTGNKTVQDYATKFLKECIDNGADGFRFDGAKH
IETTADSGFGSDFWPTVLNATTSYAKSTRGVTPFYYGEVLDKTTGNDDQSNGQSIVNSYT
SLMSITLSSVSNSIRNAVNSNNAKGATRSDFDLDDGSKAAGNKSVLWNESHDTYQAGSSS
NVGNANMDKTWALVGTRQQACGMYLARPNNWGSAMMGQADVTNWADETVKAINQFKNAMI
DQSEYLSAENGVAYNERGTKGVVLVNCGSNNVNVTAHNMANGTYNDVITGNEFQVANGKI
SGTIGSSGVAVVYDVKTGPLNTISQSGGSFKAQTLSLTLGLKDATSGTYQIDNGTVKTYT
GTKTITIGKGVSYGSTITVKLTATDGTDTSNASYTFKKVDPDQIQKIYFDNSSYNWSSVY
AYIYNDTDSVAEWPGKQMTKDSSTGYYVVEVPDEFANGSVIFTENSTATTNRYPADMEPG
LELSGSSMKFSANHKWEEYTQQTTTTSKTNPTTATTAPSRTYLYGDLNFDNQINVKDAVK
VSKYTVSKITFTDVQKKAADINGDGSIDVKDATLIQKYGIKLVDTFPVGTTFSYNDSTAP
TTATTKPTTATTTTTATTAPSGNTIKIDMSAIATGTERWAAYLWNDTDSVWVDIKDNTLS
VPSGYENLIICRMNGATTENNWDNVWNQSDNLKVSGGTTYKATGWGSDNLFSGTWA

Enzyme Prediction     

No EC number prediction in MGYG000003990_01826.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	67	357	1.2e-93	0.9887218045112782

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	2.18e-102	58	426	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	1.94e-30	61	368	4	253	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.
cd14256	Dockerin_I	3.02e-17	704	758	1	55	Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
cd11316	AmyAc_bac2_AmyA	4.65e-17	127	241	64	189	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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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	2.05e-16	60	160	1	97	Alpha-amylase domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT06294.1	0.0	1	896	1	909
CDM67953.1	1.41e-107	43	677	34	664
AWB44629.1	4.56e-107	47	665	47	646
CDM67894.1	4.49e-106	48	679	42	677
QBK21217.1	5.38e-101	53	662	44	641

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	5.16e-80	56	493	3	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	7.85e-78	53	493	3	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1UA7_A	3.73e-77	56	493	3	420	ChainA, Alpha-amylase [Bacillus subtilis]
1VIW_A	1.53e-15	61	281	13	225	TENEBRIOMOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]
1CLV_A	2.69e-15	61	281	13	225	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	1.76e-95	53	662	44	641	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	1.82e-65	52	499	47	467	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	2.77e-57	48	650	137	780	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
O97396	7.84e-20	61	360	31	313	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1
P41131	9.95e-17	58	241	25	203	Alpha-amylase OS=Aeromonas hydrophila OX=644 GN=amyA 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
0.000351	0.998894	0.000181	0.000211	0.000170	0.000152

TMHMM  Annotations     

start	end
7	29