CAZyme Information: MGYG000000915_00403

Basic Information

• Species: Clostridium nigeriense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium nigeriense
• CAZyme ID: MGYG000000915_00403
• CAZy Family: CBM26
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1206		135042.99	4.8883

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000915	3503945	MAG	China	Asia

• Gene Location: Start: 443472; End: 447092 Strand: +

Full Sequence      

MKKFLVKKFALLLSVLFITFTFLTSNFYSNQKVFASQSDLLVHFYKPSDWNNPNIYYYGD
TLSGPTWPGTTMSVESDGWYNYTIKNASTSRVIFNDGSVKQIPSAGQAGFSVSSEVWYKD
GQITTHKPNSTKNEVNIYVEKPDNWNDIWIWYDSDLSTTAWDTTSLKSYPGDMINYRSSW
YKKTIQANGKIQFLFNDGTWSKKLQNNGVDFTTDKDIWISKSGAISYEDPLKESTITPTA
IKLIASDSINVGESISVNSYITYSDGSEKQEIVNWSISDTSLASLSTSTGISTNITGIKA
GKVIITANINNLSLTKEITINDLSSNFIKVFFKSNWSSNKIYYWATVPTITTKSWPGVDM
ISEGDGWYSYTFNGTTSTNLIFNNGAGSQTGDLTRTSGTWYYYNNSWTDKDPRIDLIAPT
ITASPQAGKYESSSLNISLSAKDNSDSSPKIYYTTDLTEPTNNSILYTSEIIINKDTTIK
AIAIDKSGNVSSVYTLGYSLNNDITAPIVIASPSSGRYLTSQKVKFTITDNKDSNPLLYF
TTDGSKPELTEKYLYKGQEIYISEDTKIYTIAIDSSGNKIENYFIYNIGEVKENDFREET
IYFVMTTRFYDGDPSNNVHCWDDTTAKNPDSDPAWRGDFKGLTDKLDYIKALGFSAIWVT
PPVKNASGYDYHGYHAINHSEIDPRYKTKYDTSAEESYQKFINAAHAKGMKVIQDIVLNH
TSNFGEENLFPMFRRLNPTGLNETISTGLSKIENSKLPSNYDTLTPALQYSSRINAMKEN
SSDTDNIYHHEKSLEWEGYTVQTGQIAGDCVDLNTENPTVSDYLIDSYSKYINMGVDSFR
IDTVKHISRLTFNNEFIPKLKAEGGDDFYMFGEVCTRVRDVWNRGIPALSAPFYTWKENK
NYAWGDRVTNESSTLKAYNDNLSVSNQPTSTNAFLNGNTYKTPDYSMKSGLDVIDFPMHW
NFVNARDAFRVAVEGDAYYNDATWNVTYVDSHDYAPDTAPENQRFALGQDVWAENLSLMF
TFRGIPTLYYGSEIEFQKGKSIDVGPNAPLSQTGRAYFGDYIEGTVETTDFGLYSNASGT
MAETLANPLAKHITRLNRIRRAIPALQKGEYSVKDITGDGMAYKRRFTDTESGVDSFVLV
TVSGSATFNNIPNGKYVDAVTGEVINVTNGILLANCSGKGNLRVFVLDLPGNPAPGKIGE
DTKYMY

Enzyme Prediction     

EC	3.2.1.1	3.2.1.98

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	636	1039	1.8e-159	0.997624703087886
CBM26	42	106	1.5e-20	0.9066666666666666
CBM26	330	395	4e-18	0.9466666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	8.99e-129	597	1103	1	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.
cd11320	AmyAc_AmyMalt_CGTase_like	3.72e-50	595	1033	1	348	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.
cd11340	AmyAc_bac_CMD_like_3	3.41e-48	600	1047	5	366	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.
pfam00128	Alpha-amylase	1.04e-39	637	1034	1	326	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
COG0366	AmyA	6.66e-37	600	1034	2	356	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDY82638.1	0.0	328	1205	75	947
AET61000.1	0.0	328	1205	75	947
ASR47411.1	0.0	328	1205	75	948
AIQ71010.1	0.0	334	1205	312	1175
APB78307.1	0.0	328	1205	76	948

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6WNI_A	1.32e-33	597	1192	32	513	ChainA, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNI_B Chain B, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNU_A Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus]
6CGT_A	7.33e-28	593	1169	9	468	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]
1CGT_A	9.70e-28	593	1169	9	468	ChainA, CYCLODEXTRIN GLYCOSYL-TRANSFERASE [Niallia circulans]
3CGT_A	2.98e-27	593	1169	9	468	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans],8CGT_A Chain A, PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) [Niallia circulans],9CGT_A Chain A, PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) [Niallia circulans]
1CGU_A	9.12e-27	593	1169	9	468	ChainA, CYCLODEXTRIN GLYCOSYL-TRANSFERASE [Niallia circulans],5CGT_A Chain A, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans],7CGT_A Chain A, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	1.87e-29	595	1185	743	1194	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P08704	3.65e-28	595	1169	39	532	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P14014	1.51e-27	593	1187	43	515	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA PE=3 SV=1
P31747	2.65e-27	587	1169	37	502	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 6.6.3) OX=29335 GN=cgt PE=3 SV=1
Q05884	3.29e-27	624	1145	84	565	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 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
0.001232	0.996936	0.001233	0.000219	0.000184	0.000171

TMHMM  Annotations     

start	end
9	28