CAZyme Information: MGYG000002874_00877

Basic Information

• Species: UBA1777 sp002320035
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA1777; UBA1777 sp002320035
• CAZyme ID: MGYG000002874_00877
• CAZy Family: GH13
• CAZyme Description: Neopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
578	MGYG000002874_9|CGC1	66671.49	4.6729

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002874	2306396	MAG	United States	North America

• Gene Location: Start: 5682; End: 7418 Strand: +

Full Sequence      

MQFFDYEIEHRARYPWQFVQGKSCTLRLRCNEPVLKITVLHGDPFWFAEGEKKEPVLEET
EVSSKQLLLDDTYYSVTIPVQTHKLRYHFAITLYDGTTLMLSELGVTDELPESQIRPFMV
PYVFEREHYCAPDWAKNFVWYQIFPDRFAGEGDPAAFAPTRDNFFGGTLKGITGKIPYLK
DLGVRGIYLNPIFQSPSNHRYDTADYARIDSLLGDEKDFCQLVESLHEAGLRIMLDGVFN
HCAWDHPFWQDVLQNGESSPYYEWFYIEDVRSLTGAEKEKFSPEIIKRDHPFACFAFAAN
MPKWNTENELVMDYLIGQAEHWTRDYGIDAWRLDVPDEISMRFLREFKRRIRAVSDQVYI
IGEIWQDAGLWLDYSVFDGAMDYPLYYAIRDFAMTGQDNLAAFARRIQRWVISSPEAVHP
YQWAFCSNHDIPRLLTECGGDAERAKLALFLTAVLGGNMSAYYGDELGMEGADDPDNRRA
MAWGQINKSWYSFYTKLIRLKREELNECKIMHISLQDALTITLSNSTGNKLLAVVSPVDQ
PVLFEVATNCEFLFGKADVTAVGTEVRGFALFQVSAEE

Enzyme Prediction     

No EC number prediction in MGYG000002874_00877.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	167	475	7.3e-104	0.9966666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	8.24e-156	139	504	3	381	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	4.20e-80	54	502	41	521	maltodextrin glucosidase; Provisional
pfam00128	Alpha-amylase	3.35e-64	167	475	1	334	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	8.81e-64	139	477	2	366	Glycosidase [Carbohydrate transport and metabolism].
cd11316	AmyAc_bac2_AmyA	2.73e-63	139	503	2	396	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLF55867.1	1.70e-111	8	556	6	568
QIZ66829.1	2.22e-110	8	535	6	534
AMX84416.1	2.45e-109	8	535	6	534
QLL99027.1	4.10e-109	8	556	6	568
QNU27305.1	1.91e-108	8	535	6	534

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1SMA_A	7.67e-109	8	576	6	587	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
1J0H_A	1.52e-108	21	540	20	540	Crystalstructure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0H_B Crystal structure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0I_A Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus],1J0I_B Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus]
1J0J_A	4.25e-108	21	540	20	540	ChainA, neopullulanase [Geobacillus stearothermophilus],1J0J_B Chain B, neopullulanase [Geobacillus stearothermophilus],1J0K_A Chain A, neopullulanase [Geobacillus stearothermophilus],1J0K_B Chain B, neopullulanase [Geobacillus stearothermophilus]
1GVI_A	1.19e-107	8	576	6	587	Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.]
1BVZ_A	5.59e-96	8	501	6	494	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
A0A7U9P668	8.33e-108	8	576	6	587	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1
P38940	4.61e-107	21	540	20	540	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
P32818	3.78e-101	8	547	6	553	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 SV=1
Q08751	3.06e-95	8	501	6	494	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
Q08341	3.58e-95	8	502	7	497	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
1.000074	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002874_00877.