CAZyme Information: MGYG000001507_02572

Basic Information

• Species: Paenibacillus ihuae
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus ihuae
• CAZyme ID: MGYG000001507_02572
• CAZy Family: CBM35
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1173		126700.21	5.7325

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001507	6631509	Isolate	not provided	not provided

• Gene Location: Start: 2719821; End: 2723342 Strand: -

Full Sequence      

MVRNKTRRFLSWFIIFALCFSLFGAAGGASASNTNYTVTYTNTTATAVTLHWTTNNWTTL
TDTVMTKSGTTFTANITVAEGATLTYCYHITAPTDSWDNNSGKNWSVVIPAAGKYEAESV
VLSGGAKVNTNHTGYSGTGFVDGYTASGASSTFTVQASAAGAYNATLHYANASGSAKTLS
VYVNGTKVKQTTLANLANWDTWSDQTEPLTLMAGNNTIAYNYDGDDSGNINIDYVMIQPG
ISPTPTPSPTPTPTPSPTPTPTVTPTVTPTVTPTATPTVTPTPTSTATVSPTPTSTATGI
TVHIKKPSTWNSAVRIHYWNMNPSTVPISGAWPGILMNSDGNDWYSYTIAGAAGTSLIFN
DSNGKQTADLARTVKESWYYTDNVWYETNPEAPKIPVITVSPAPKTYDSAQTIALSSSNS
SDKIYYTTNGSTPTTASPLYTSPIQVSSSLTIKAFGVNTSGQGGSVASFAYVIDLNADLQ
APTITANLPVGQSTTAVTVSFNIKDNKAATTSAYYTDDGTEPTSGSKAYISGNALAGLAG
PSILISKTTTLKFLVIDAAGNRTTQNFVYSIGNKGDFREDSIYFVITSRFYDGDTSNNVH
AWDDAKAGNPDSDPAWRGDFKGLIQKLDYIKALGFSAIWITPVVQNASGYDYHGYHAINF
AKVDPRYESAGASYQDLITAAHARGIKVIQDIVVNHTGNFGEENLFPMFKKDATKADTIA
NLLKITDKLPANYDTMTPDQQYQARLALMKTAETNNNIYHTEKSLSWESYTVQTGQIAGD
CVDLNTENPVVNQYLIDSYNQYIDMGVDAFRVDTVKHVSRYIFNKYFVPAWKARGGSNFF
IFGEVATRYRDVWNSGIPAISTPFYTWKSAKSYPGDGQNDYASNKLSVEQEWADNSTTAG
QPTSNNAFLNGNTYHAPDYSMKSGMDVIDFPMHWAFKSAQEAFSMRSGDQYYNDATWNVT
YVDSHDYAPDQAPENQRFAGTQDTWAENLALMFTFRGIPAIFYGSEIEFQKGKVIDIGPN
AQLSTTGRAYYGDHIEGSVTVQDFGKYTNATGTLAESLNYPLAKHIRQLNLIRRAVPALQ
KGQYSTENVSGELAFKRRYTDASKGIDSFALVTISGNATFSGIPNGTYVDAVTGDSKTVT
NGTLTLTCSGKGNARVYVLNGSGGIGETGTYLK

Enzyme Prediction     

EC	3.2.1.1	3.2.1.98

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	617	1012	3.3e-179	0.997624703087886
CBM35	115	236	3.7e-35	0.9831932773109243
CBM26	301	370	1.1e-19	0.9066666666666666

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	2.44e-137	578	1076	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	3.52e-57	576	1006	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.
cd04083	CBM35_Lmo2446-like	2.99e-53	113	235	1	123	Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.
cd11340	AmyAc_bac_CMD_like_3	5.39e-49	579	1020	3	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	3.95e-44	618	1007	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSF42489.1	0.0	1	1173	1	1173
CQR58204.1	0.0	1	1173	1	1183
AIQ47465.1	0.0	1	1173	1	1190
AIQ52956.1	0.0	1	1173	1	1184
AWV35903.1	0.0	1	1173	1	1183

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6CGT_A	2.15e-27	570	1144	5	476	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]
1CGT_A	2.84e-27	570	1144	5	476	ChainA, CYCLODEXTRIN GLYCOSYL-TRANSFERASE [Niallia circulans]
3CGT_A	3.76e-27	570	1144	5	476	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans],8CGT_A Chain A, PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) [Niallia circulans],9CGT_A Chain A, PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) [Niallia circulans]
4CGT_A	1.49e-26	570	1144	5	470	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]
6WNI_A	2.54e-26	578	1099	32	452	ChainA, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNI_B Chain B, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNU_A Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	2.39e-34	576	1151	743	1189	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P08704	8.79e-30	576	1147	39	538	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P31747	1.44e-27	570	1006	39	397	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 6.6.3) OX=29335 GN=cgt PE=3 SV=1
P30920	1.78e-26	570	1144	39	510	Cyclomaltodextrin glucanotransferase OS=Niallia circulans OX=1397 PE=1 SV=1
P14014	4.10e-26	570	1134	39	496	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA 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
0.002787	0.996149	0.000289	0.000371	0.000191	0.000176

TMHMM  Annotations     

start	end
9	31