CAZyme Information: MGYG000000392_01780

Basic Information

• Species: Ruminococcus_E sp003521625
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp003521625
• CAZyme ID: MGYG000000392_01780
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1195	MGYG000000392_15|CGC1	129631.64	4.5247

Genome Property

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

• Gene Location: Start: 20962; End: 24549 Strand: +

Full Sequence      

MKRKGLLKCFSAVLVLCMILSCVSFSFATAGAAVVGETSIVSASSSASGDNFTWDNASVY
FLLTDRFKNGNTSNDHSYNRGLDQDGNVVSGIDTRGTFHGGDFAGVTQAINEGYFNDLGV
NAIWISAPYEQIHGYVVGGDGNPSYAHYSYHGYYVLDYTQTDANFGTAEEFGTLVDTAHE
HGIRVILDVVMNHSGYNSLYDMDEYGFGTVKSGWENYYFSHQNINNADYHSYIDYDSSAA
DWANWWGADWIRCGVAGYTQGGGDNLTMSLAGLPDFRTDSTATVGIPNLLKTKWKKEGRL
SQETNELSSYLSKTGKKQTVTNSISYWLSTWVREYGVDGFRCDTAKHVDLASWKTLKDTC
VDALKEWRQNNPSKAGADWDEDFWMTGECWDHNIGWGYDSYYTQGGFDSMINFETQGGGM
LSMSGLNGVYSNYASSINSNDKFNQLSYLSSHDSTLARGNLISTGSAFLLLPGGIQIYYG
DETNRPLVPGVPNDGNGGAGHSLRSDMNWDSADSAVLAHWQKVGSFRNKHVSIGAGDHQQ
ISGYSSSTGYTFSRSYDNGVISDNIIATIGAPSNTNLAVDVSSLWSDGTIVTNAYDGTTA
TVTNGKATFNTGANGTILMEGPVSTISMSLKGSYSFYDSQTLTVSLRGADYAMVSIDGGT
EFKVVDGDKFSIGEGVEVGATIKVTMTASNDEETSTKSFTYKKKDPNAVVRVYFDNSRYN
WSTVNAYIYDESSGNAVENKDWPGETMTYDTATGFYMIEVPDNLTNGRVIFNAGKTSSNR
YPADGAQGLEINGTHMLFSYGNKWEPYTNQTVGPTEPTTAPDPTKTTTVYFDNSNSKFST
PTIYYWSYATNSSPVSWPGVPMTNVSGDIWKATFDNKYDGCIFSNNGSNKIGDLTIPGSN
YIHNGSSWSAYTEPTEPTEPTTAPATTVPVTTAPVTTVPATTAPATTVPATTVPATTVPT
TDELTVKASSNIFPTATKTFNKDEGTVTVSYKLTANMKAVDTQWTLTYDNTKLKYDIADN
MVDGSQTITPSAGDKLVFNNKSNYIKGNFSNLKLVSFDNNADFVSVTFDIIGTGKADVYL
DLEVLSLAYKDSSNKPHCASIVDFSKMQDISGIKGFENASISTSTNLESSILMGDVNGDG
YVKVDDATAVLKYVVGKESLNSLQIKAADVNRDGKVNVKDATLIQKYLADMISGF

Enzyme Prediction     

No EC number prediction in MGYG000000392_01780.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	101	483	3.8e-142	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	52	558	185	672	alpha-amylase; Reviewed
COG0366	AmyA	9.31e-40	57	561	1	477	Glycosidase [Carbohydrate transport and metabolism].
cd11320	AmyAc_AmyMalt_CGTase_like	5.09e-39	59	527	7	387	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.
cd11339	AmyAc_bac_CMD_like_2	8.35e-39	58	530	4	344	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.
cd11338	AmyAc_CMD	1.26e-37	65	537	10	388	Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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
QCT06045.1	0.0	48	926	51	910
BCN30960.1	5.50e-283	50	898	56	885
QCT06087.1	6.60e-210	29	620	28	641
CDM67955.1	2.63e-209	36	790	52	809
CDM67952.1	1.36e-200	52	772	74	800

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	3.94e-23	53	557	5	389	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	5.89e-23	53	557	39	423	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	1.26e-22	53	537	6	372	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1A47_A	5.14e-20	59	361	17	248	CGTASEFROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR [Thermoanaerobacterium thermosulfurigenes],1CIU_A Thermostable Cgtase From Thermoanaerobacterium Thermosulfurigenes Em1 At Ph 8.0. [Thermoanaerobacterium thermosulfurigenes]
1CYG_A	8.87e-20	51	194	8	137	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	6.51e-116	52	536	184	646	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P31797	1.31e-19	24	194	10	168	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
Q05884	1.75e-19	95	482	92	462	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P26827	2.27e-19	34	361	18	275	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2
P05618	2.72e-18	51	194	38	168	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1011) OX=1410 GN=cgt PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.001082	0.488602	0.509324	0.000510	0.000238	0.000208

TMHMM  Annotations     

start	end
13	35