CAZyme Information: MGYG000001659_02544

Basic Information

• Species: Paraprevotella sp900760455
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella sp900760455
• CAZyme ID: MGYG000001659_02544
• CAZy Family: GH13
• CAZyme Description: Neopullulanase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
559		64009.6	6.069

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001659	3410285	MAG	United States	North America

• Gene Location: Start: 18361; End: 20040 Strand: +

Full Sequence      

MIFKQKIIVYQVFTRLFGNNNAHCVPNGSIEENGCGKMAAFTAEALGQIRELGATHIWYT
GIIEHATQTDYSAFGIARDHKAVVKGKAGSPYAIKDYYDVDPDLAKNVDERMKEYLSLVK
RTHRAGLKMVIDFVPNHVARQYHSDARPEGVKDLGEEDNCQLAFHPQNNFYYIPGEELHA
DFDLQQGENEPYREIPAKATGNDNFSAWPNRNDWYETVKLNYGIDYCGGHRRCFSPVPDT
WYKMRDILLFWAATGIDGFRCDMAEMVPAEFWGWAIPQVKAKYPDLIFIAEVYNPAEYRN
YIFNGHFDYLYDKVGLYDTLRGVTCGYLPANAITGCWQSVDDIKEHMLNFLENHDEQRLA
SDFFAGNALKGKAALLVSACMGTNPMMIYFGQELGERGMDAEGFSGRDGRTTIFDYWSID
TIRRWRKGKLSNEEKSLQDFYANVLRICNEEKAIREGQFYDLMYVNPTNEHFNPEKQYAF
LRRSHKELLLIVANFDAQEQLTDVRIPKHAFDFLNIKEKSELPAKELLSGKKESITLTPD
IPITVKLPAHGGIILKIKI

Enzyme Prediction     

No EC number prediction in MGYG000001659_02544.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	33	400	6.6e-182	0.9973333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	7	454	1	456	Alpha amylase catalytic domain found in an uncharacterized protein family. 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.
cd11313	AmyAc_arch_bac_AmyA	1.04e-48	8	457	6	336	Alpha amylase catalytic domain found in archaeal and 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 firmicutes, bacteroidetes, and proteobacteria. 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.
cd11347	AmyAc_1	1.32e-41	8	460	2	390	Alpha amylase catalytic domain found in an uncharacterized protein family. 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	2.11e-25	8	508	2	494	Glycosidase [Carbohydrate transport and metabolism].
200451	cd00551	1.52e-23	8	396	1	259	AmyAc_family Alpha amylase catalytic domain family. 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; and 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 this 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJR54587.1	1.89e-293	4	559	4	565
AII70030.1	1.89e-293	4	559	4	565
QJR73493.1	1.89e-293	4	559	4	565
QJR60612.1	1.89e-293	4	559	4	565
QUT85123.1	1.89e-293	4	559	4	565

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	3.45e-17	36	361	27	284	Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
1JF5_A	9.84e-17	5	508	129	547	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF5_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1WZK_A	9.84e-17	5	508	129	547	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZK_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]
1JF6_A	1.30e-16	5	508	129	547	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1BVZ_A	1.30e-16	5	508	129	547	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q08751	7.14e-16	5	508	129	547	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
P38940	1.06e-12	10	510	138	550	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q59226	2.34e-12	8	496	132	535	Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
Q9JN46	4.34e-12	130	293	231	408	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2
P14899	6.32e-12	8	548	36	499	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2

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
0.999423	0.000591	0.000016	0.000002	0.000001	0.000003

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001659_02544.