CAZyme Information: MGYG000003875_01811

Basic Information

• Species: Firm-11 sp900540045
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-11; Firm-11 sp900540045
• CAZyme ID: MGYG000003875_01811
• CAZy Family: GH13
• CAZyme Description: Neopullulanase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
583		67579.72	6.0996

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003875	3247365	MAG	United States	North America

• Gene Location: Start: 68133; End: 69884 Strand: -

Full Sequence      

MRTIQFGSIYHMPWLEYRHALPDGRVCLRLKTGRGEFSRVAVRVTSNYAMPDYFKGADEY
EMAVAYRDEWHDFYEVIFSPRDLRIKYLFVLQSDELTFKLDATGLKAGADAEEDVSQAFA
FAYVYPADPMPEWARGCVGYQIFPDRFRREPVETDTEPVEPWTSTRVQNQYRFGGNLRGI
LKAVPYLKDLGVKMIYTTPLFLSDSSHRYNTFDYFKIDPLLGTEDDLRALCDELHKNDMR
IVLDGVFNHSGLKFAPFVDAMEKGEASPYRGWFCFDDKMPYGYHTFGDWRYMPKLNLQNE
DCAQYFLSVGRYWLEKCRVDGWRLDVSPEVWPDFWRQFKTMMRKVNPDSLMVAECWDDSR
EWLTVGDMFDSTMHYVLSRNIWSRFCRHEISTAQFDCALNRAAMLYPQRTQEVLWTFLGS
HDTQRIRTRAGGDLRMVHAASFFQFTYLGSPIIYYGDELGMEGGEDPDCRRPMRWDDVEG
NPTRAHYQKLARLRAQLPALRTGRFRSHVALENGLYAFRRETDTQQLLCVVNTGLEPVSV
RLELPGGMAGMAAVHDHYTGRSLAVADGGVHISLKVGEGLILE

Enzyme Prediction     

EC	3.2.1.-	3.2.1.54

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	175	467	1.7e-105	0.9966666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	1.62e-172	138	505	3	389	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.
PRK10785	PRK10785	1.59e-90	25	544	22	568	maltodextrin glucosidase; Provisional
cd11316	AmyAc_bac2_AmyA	3.10e-69	175	503	20	403	Alpha amylase catalytic domain found in bacterial 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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.
cd11353	AmyAc_euk_bac_CMD_like	9.98e-68	177	505	29	366	Alpha amylase catalytic domain found in eukaryotic and 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 mainly 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.
COG0366	AmyA	1.85e-63	138	550	2	500	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAA02473.1	6.38e-127	8	582	5	581
CAY02972.1	6.38e-127	8	582	5	581
CAZ78903.1	6.38e-127	8	582	5	581
BAA97040.1	6.38e-127	8	582	5	581
BAB40638.1	6.38e-127	8	582	5	581

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1BVZ_A	2.33e-128	8	582	5	581	Alpha-amylaseIi (tvaii) From Thermoactinomyces Vulgaris R-47 [Thermoactinomyces vulgaris],1BVZ_B Alpha-amylase Ii (tvaii) From Thermoactinomyces Vulgaris R-47 [Thermoactinomyces vulgaris],1JI2_A Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 [Thermoactinomyces vulgaris],1JI2_B Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 [Thermoactinomyces vulgaris],3A6O_A Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex [Thermoactinomyces vulgaris],3A6O_B Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex [Thermoactinomyces vulgaris]
1JF6_A	6.56e-128	8	582	5	581	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1WZM_A	6.56e-128	8	582	5	581	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZM_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]
1JIB_A	1.31e-127	8	582	5	581	ChainA, NEOPULLULANASE [Thermoactinomyces vulgaris],1JIB_B Chain B, NEOPULLULANASE [Thermoactinomyces vulgaris],1JL8_A Chain A, ALPHA-AMYLASE II [Thermoactinomyces vulgaris],1JL8_B Chain B, ALPHA-AMYLASE II [Thermoactinomyces vulgaris],1VB9_A Chain A, alpha-amylase II [Thermoactinomyces vulgaris],1VB9_B Chain B, alpha-amylase II [Thermoactinomyces vulgaris],2D2O_A Chain A, Neopullulanase 2 [Thermoactinomyces vulgaris],2D2O_B Chain B, Neopullulanase 2 [Thermoactinomyces vulgaris]
1WZK_A	1.31e-127	8	582	5	581	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZK_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q08751	1.28e-127	8	582	5	581	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
Q59226	1.04e-115	8	532	5	533	Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
P32818	1.66e-115	8	583	5	585	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 SV=1
P38940	2.14e-113	8	531	5	534	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q08341	1.48e-107	4	540	2	543	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000052	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003875_01811.