CAZyme Information: MGYG000002482_01192

Basic Information

• Species: Ruminococcus_E bromii
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E bromii
• CAZyme ID: MGYG000002482_01192
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1063	MGYG000002482_56|CGC1	114272.58	4.4139

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002482	2151595	Isolate	United States	North America

• Gene Location: Start: 68606; End: 71797 Strand: -

Full Sequence      

MKKAKKIASLVVASALLTSSFAAITSVNAAEIDSAQVASADNTLRDKVGDGVMLHAFNWS
YNTIKENLPAIAAAGYTTVQTSPVQQPKDYSTSGDVVGQWWKLYQPISFHIAEKSWLGTK
DDLKSLCDEADKYGIKIICDIVSNHVANADDDKPNAVSSQVKQYEPDFYKKRKTLTRYSY
KGDASDSSVQAVVQGHVSRCPDLVTNDTVIQNYIINLLKECIDCGVDGFRFDAAKHIETE
DDGEYASDYWKNVTTSASSYYTQKTGNDLYIYGEILNNCGAGRSYNSYTKYINVTDNRTG
DAVLYNVAKGKASSAANATYQSGVAASNAVIWAESHDTYEGNSGSWGYSNTSSVSDENVV
KAWAIVASRKDSTALFFARPGTALMGNVSTDSTYKSTAVSEINKFHNLFVGQSEKLGSSG
DIAYVARGTSGIVLSNCKGTNASVSISGTGLADGKYTDTVSGAEFKVVNGVLTGSIGKTG
VAVVYNGTTTPKVTNSVESGTFKGDTMTLTLGLENAASGTYCLDDSTPVKFTDTTSIRIG
SDYKPGETINLTVTATDGVKTTSTVYKYTKSTAEESGVYVFFNPATKKNWSAPYQVYIYD
ENTDKGMVYKNANWPGEAMTLDPATGYYYYEVPKSSCISADEDDQNQAASNFDLSSSANT
RVIISEKGGEQYPGRTDAAISLNGSSKAYSLSKAGTWEDTTLTPTKVEIEATDVTKGTAT
EPTTEAQTTAPVPATDPTQPDTKPSQPSGGAVYGDVNNDGIISVVDSTLVQKFIVHNESL
TTEQQIIADVNGDNVVSVVDATAIQKYIVHSEGSGRTGEAYTTVEPTTAEPTTAKPTEAP
ATAEPTTKPADTYTLYFKTKLGWMTSDGVSLFAYDLDTGVSYQLEQDTDAYPNVYTAEVP
ATVTNVSVYRNLSEVDEKPVGGDDGNVYNCWDATVSKTNNCITLSNDEAVSTAPYAPEQK
PAFTLSRVYFDNSKANFSDVYIYGWAESGLNETAVHMNKIAGTDIWYYDFDTPLSPGANC
FLFKDTESTWETQTNDLTVADGKNCFRANPGSKSGGVWVSYSE

Enzyme Prediction     

EC	2.4.1.25

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	59	342	2.6e-81	0.9887218045112782

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	3.11e-132	50	416	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	2.11e-28	51	345	2	245	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.
COG0366	AmyA	1.32e-18	43	276	8	240	Glycosidase [Carbohydrate transport and metabolism].
cd14256	Dockerin_I	1.38e-16	753	809	1	57	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.
cd00551	AmyAc_family	4.49e-15	61	388	24	254	Alpha amylase catalytic domain family. 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; and 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 this 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
QCT06294.1	1.90e-114	44	785	52	743
QLY40627.1	3.61e-95	44	571	78	594
CDM67953.1	8.98e-88	36	634	35	623
CDM70432.1	2.37e-86	39	570	42	564
QDY86356.1	1.17e-80	33	633	37	614

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UA7_A	3.23e-69	48	485	3	420	ChainA, Alpha-amylase [Bacillus subtilis]
3DC0_A	4.43e-69	48	485	3	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	9.06e-69	48	485	6	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1G94_A	5.81e-11	54	241	6	183	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]
1AQH_A	5.91e-11	54	241	6	183	ALPHA-AMYLASEFROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis],1AQM_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS COMPLEXED WITH TRIS [Pseudoalteromonas haloplanktis],1B0I_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	5.37e-73	34	684	32	646	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	7.72e-64	39	529	42	502	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	8.87e-49	40	640	135	760	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P22630	1.95e-16	52	433	23	407	Alpha-amylase OS=Aeromonas hydrophila OX=644 PE=3 SV=1
P41131	5.31e-16	50	241	25	207	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
0.000216	0.999114	0.000161	0.000177	0.000154	0.000134

TMHMM  Annotations     

start	end
7	29