CAZyme Information: MGYG000002414_05115

Basic Information

• Species: Paenibacillus odorifer
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus odorifer
• CAZyme ID: MGYG000002414_05115
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1000		107343.69	5.1898

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002414	6802552	Isolate	South Korea	Asia

• Gene Location: Start: 5749508; End: 5752510 Strand: -

Full Sequence      

MKRKLWYVPVLITSILLSTVINLFVLAPQADAASIGTINENDTIYQIMVDRFNDGDSSNN
ATGAAIRYGENSEEDFRYMKGGDWQGVIDKLSYIKNMGYTAIWISPVAEPQMTNRENNGS
GKNTAYHGYNVKDPNAANPYFGTKEKLKELVDSAHAVGIKVVIDVVPNHIGDYMLGTQAY
YDIPSLQPAAPFNNPAWYHHNGDINWSLADGRYDQWAQDYLENHDLGGLDDIDFDVPAAK
KAVFDSIKGWFDYTGADGARVDAAKLMKPTDIGELQNYLGVNTFGENFDGNAEFVSRWVG
NNKEWGMLDFPMFFSVLNSFAYGQSFDSNIKSTLAQDSYYNGNANHMVTFIDNHDRNRFL
TEAGGSVDKLQNALSFIFTVRGTPVVFQGTEQNKGNGNGQIMTGGIADTWNRWSMVKRDA
NGNVIENYFNENASTYKHVAKLNEIRKNNPALRTGTQREMWSAQNLYAFSRRIDTGTNLG
QEVISVFSNKSSGSQTVTIPLRAESSLAVGTVLYNQLNTSDTVTVQSGGATGKQITVTVG
ANAAKIYAKQQLPTDTVAPTVPTNVTATVQNASSALVSWTASTDNVGVTGYEIYRNGVKV
GTSATTSYTDNGLSASTTYDYTVKAMDAAGNLSLLSAIASVTTPAGNSVTIYYKQGYTSP
YIHYRPAGGTWTTSPGVAIPVSDVAGYNKITINIGSASQLEACFNNGSGTWDSNGGSNYL
FSAGTWTYTPTGNIQSGGPVTPTPTVTPTPTPTPTVTPTPTVTPTPTPTVTPTPTVTPTP
TPTPTVTPTPTVTPTPTATPVGSTATIYYKNAAYSSSYIHYKLDGSTVWTTSPGEQLQAS
AFTGYKAVTIQLDTAAGLTAAFNNGSGTWDNNGGNNYHFAAGTWSIVNGNITAGEPQADS
VTFRVTVPASTPVSGPVYLSGSFNSWNAADPNYQLTKGSDGIYSITLSLPAGTAIQYKVT
RGAWTNVEVNSNGSDLSNRTLTPSGGAQTVNLTVQRWKDL

Enzyme Prediction     

EC	3.2.1.1	2.4.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	81	394	8.3e-64	0.9705882352941176

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11320	AmyAc_AmyMalt_CGTase_like	1.19e-158	40	448	3	389	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	4.03e-74	42	449	3	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.
cd11319	AmyAc_euk_AmyA	4.73e-72	43	448	10	371	Alpha amylase catalytic domain found in 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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	1.60e-61	42	448	4	407	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	4.32e-60	82	398	1	332	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
AWV35694.1	0.0	1	1000	1	1000
AIQ76409.1	0.0	1	1000	1	1019
AIQ25945.1	0.0	1	1000	1	1003
AIQ37748.1	0.0	1	1000	1	1019
QSF46674.1	0.0	1	999	1	984

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1CYG_A	3.53e-56	32	494	1	436	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
4CGT_A	2.34e-54	42	722	15	664	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]
1CGT_A	1.15e-53	42	722	15	670	ChainA, CYCLODEXTRIN GLYCOSYL-TRANSFERASE [Niallia circulans]
6CGT_A	1.15e-53	42	722	15	670	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]
3CGT_A	6.95e-53	42	722	15	670	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans],8CGT_A Chain A, PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) [Niallia circulans],9CGT_A Chain A, PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0P8X0	9.69e-182	555	999	811	1289	Alpha-amylase OS=Niallia circulans OX=1397 GN=igtZ PE=1 SV=1
P21543	1.56e-73	26	549	731	1196	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P14014	1.85e-55	27	725	31	707	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA PE=3 SV=1
P31797	3.05e-55	32	494	32	467	Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P30920	1.00e-52	42	722	49	704	Cyclomaltodextrin glucanotransferase OS=Niallia circulans OX=1397 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
0.000383	0.998912	0.000180	0.000198	0.000166	0.000156

TMHMM  Annotations     

start	end
5	27