CAZyme Information: MGYG000000163_01267

Basic Information

• Species: Enterococcus_C asini
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_C; Enterococcus_C asini
• CAZyme ID: MGYG000000163_01267
• CAZy Family: GH13
• CAZyme Description: Amylopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
608		70530.09	4.7518

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000163	2560364	Isolate	China	Asia

• Gene Location: Start: 16106; End: 17932 Strand: -

Full Sequence      

MGEIYYNPWKSAYKSPFGAIQEGQSARFGFLGADSGIDQVYLVIEPEGQKAYRIKMTPQE
NGFFQTEFAFNDGKGLYFYHFELEYLSANQQRFTRYYGWSGENGHGEVRDYLKECMNYQV
TCYQKVEKAPDWYRQAVFYQIFPDRFFNGNPDGRVNNPKENTFLYGDLRDDPMYIKDAQG
EVLRWDFYGGNFAGIQAKIPYLKELGVNALYLNPIFEARSNHRYDTADYLKVDPILGTEA
EFQELLDTLHQEGFRVILDGVFSHVGRHSRYFNYDGAYGPGVGAYQDIKSPYFPWFTFLS
YPNEYRSWWGVKDLPEVNKENEEFQRFIYGAKGVLSKWNQMGLDGWRLDVADELPDEFIA
GIRNNLDHYEDKVLLGEVWEDASNKVSYGVRRQYILGDHLHGVMNYPLRSATIDFLMENC
SPEDIALVFTRLQENYPREVFYNSLNNIGTHDTERILSQLEGDYEKLSLAFALLVTFPGV
PCIYYGDEAGLTGGKDPDNRKFFPWGRVDETCYRECRKWLALRKENHLLQGGEFGLIYSE
RLLGVLRYDETHFILTVLNPLGVEVIVSAKDFAAFRELPLTRERLAELLEGQRIRAHGSY
VIEGELSE

Enzyme Prediction     

No EC number prediction in MGYG000000163_01267.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	190	498	2.5e-121	0.9968354430379747

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	135	534	1	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	1.63e-104	30	540	26	537	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	1.32e-90	13	534	12	577	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11337	AmyAc_CMD_like	9.17e-61	137	534	1	328	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). 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.
pfam00128	Alpha-amylase	4.86e-59	190	497	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCA86024.1	7.08e-284	1	608	1	609
AOF48958.1	1.79e-255	1	578	1	584
AYW48729.1	1.10e-252	1	605	1	603
QZO10075.1	9.60e-241	1	604	1	609
AYW45175.1	1.87e-240	1	560	1	560

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1J0H_A	3.49e-80	128	596	127	566	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	9.54e-80	128	596	127	566	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]
1SMA_A	3.96e-77	128	596	127	566	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
1GVI_A	5.75e-76	128	596	127	566	Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.]
2Z1K_A	7.70e-75	132	540	3	405	CrystalStructure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_B Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_C Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_D Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P16950	1.14e-92	13	539	262	837	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38939	6.80e-91	4	539	248	836	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P36905	1.71e-89	4	540	251	838	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38536	9.28e-89	4	540	251	837	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P38940	1.91e-79	128	596	127	566	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT 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
1.000071	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000163_01267.