CAZyme Information: MGYG000000104_01895

Basic Information

• Species: Clostridium cuniculi
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium cuniculi
• CAZyme ID: MGYG000000104_01895
• CAZy Family: CBM26
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
863	MGYG000000104_11|CGC3	97736.1	4.3386

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000104	3679160	Isolate	Canada	North America

• Gene Location: Start: 74146; End: 76737 Strand: -

Full Sequence      

MKKLYQKLLVFLLAFTTLFSTALFSNSKYINSTYADSNTITIYVEKPSNWAEIWIWYDSD
LSTSAWDTTSLKESPGNLTEYRTDWYKKTLSSSKVQFLFNDGTWNNKLTNSGNDFITTSD
IWIKKDGSISYTDPVSESPVNTSVKVHFKSSWGQPNIYYWNTTPSFSVESWPGTSMTSEG
NDWYYYEIPNITSANLIFNGNGNQTADLSRTYGEWWFKDNQWYSSNPENVSDNDKDENDD
QDKDNNDDADKDVNTGNRTDFRDETIYFVMTSRFYDGDPSNNVHCWDDAQAGNPDSDPAW
RGDFKGLIDKLDYIKALGFTAIWITPVVKNASGYDYHGYHAINFSEVDPRYESEGATYQD
LIDAAHEKGLKIIQDIVLNHTGNFGEENLFPLFEKDSTKEDTADNLVMIDLYNRLPSNYA
SLTASEQYQARITAMKEGINDSENIYHHEKSLSWEGYTVQTGQIAGDCVDLNTENEKVIN
YLVDSYTKYINMGVDAFRLDTVKHISRLTLNNEYIPAFKEAGGEDFYIFGEVATRYRQVW
NNNIPAISTPFYTWKETKSYPWSTLAEREQSTLEHWNDNQQVSEQPTSTNHLLSGNTYHT
TDESIRSGLDVIDFPMHWNFNNARDAFNVAVSGDQYYSDATWNVTYVDSHDYAPDCAPEN
QRFAGSQDTWAENLNLMFTFRGIPAIYYGSEIEFMKGAPIDVGPNAPLSTTGRAYFGDYI
EGSVNVTDFAQYDSATGTMAETLNHPLSKHIQRLNLIRSQIPALRKGQYSTENVSGDMAF
KKRYTNAEEGVDSFVCVSITNGATFNDIPNGKYVDAITGDIKNVTDGTLSIPSVGKGNMR
IYVLDLPGNSAPGKIGEDGTYLK

Enzyme Prediction     

EC	3.2.1.1	3.2.1.98

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	301	697	3.9e-164	0.997624703087886
CBM26	145	211	2.2e-19	0.9733333333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	5.56e-135	262	761	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	9.34e-50	260	691	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	1.50e-44	265	697	5	357	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	6.80e-43	302	692	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	1.03e-37	265	692	2	356	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCJ94880.1	0.0	38	863	38	849
QEH70845.1	0.0	40	863	128	963
AET61000.1	0.0	109	863	40	948
AIQ62238.1	0.0	142	863	319	1194
ASR47411.1	0.0	142	863	73	949

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6WNI_A	5.48e-34	262	850	32	514	ChainA, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNI_B Chain B, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNU_A Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus]
5A2B_A	1.91e-27	256	844	33	482	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]
5A2A_A	2.83e-27	261	844	6	448	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	1.64e-26	261	532	7	221	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1I75_A	2.66e-26	254	860	5	497	CRYSTALSTRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN [Bacillus sp. (in: Bacteria)],1I75_B CRYSTAL STRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN [Bacillus sp. (in: Bacteria)],1PAM_A CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1PAM_B CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1UKQ_A Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose [Bacillus sp. 1011],1UKQ_B Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose [Bacillus sp. 1011]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	2.65e-36	255	831	738	1184	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q05884	5.20e-31	302	804	98	565	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P08704	6.26e-29	260	817	39	523	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P09121	1.28e-26	254	860	32	524	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 38-2) OX=1412 GN=cgt PE=1 SV=2
P27036	8.83e-26	257	827	33	487	Cyclomaltodextrin glucanotransferase OS=Bacillus ohbensis OX=1481 GN=cgt PE=3 SV=2

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
0.088403	0.834613	0.075751	0.000551	0.000330	0.000329

TMHMM  Annotations     

start	end
7	24