CAZyme Information: MGYG000000709_00010

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA738
• CAZyme ID: MGYG000000709_00010
• CAZy Family: GH13
• CAZyme Description: Amylopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
546		61981.68	4.7719

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000709	1364323	MAG	Kazakhstan	Asia

• Gene Location: Start: 9958; End: 11598 Strand: -

Full Sequence      

MIVHESRNSAFRRPFGAAETGTEVYLAAEKAGAADMTLRLHPFTGEDTLLPMASEGGGRF
SVTVTLPETPCVLWYSFRTGDDETCAWQITVYKKAAVPDWWKDGVVYQIFPDRFARERDW
TPREPEARRGTHRFLVRDWDTPVFYPRAENGDVSSWPFWGGTLRGIEEKLPYLASLGVTV
LYLNPIFEAASNHRYDTADYTRIDPLLGKKKDFESLCEAAQKRGIRIVLDGVFNHTGADS
VYFDKFGNYGTAEKYRSWFRFGEQYRHGYECWWDVPDLPNVEESDPSFREFLCGEDGVVR
RWLRRGASGWRLDVADELPDSLIRDIRTAMKAEKEDSLLLGEVWEDASNKVSYGALREYF
LGSELDATMHYPFRTAVLDFLQGKINAQTACDTFWTIQEHYPKENLYAALNLIGSHDRAR
VLTVLGGDMNALKMAMFLQFALPGVPCVYYGDETGLTGGTDPYNRGSFPWGRGDTAITDF
VRSLTAMYQETPLLRRGECEMLFFGENVLGCRRFDENGSVLALVNRGEDDAECFGVTVPG
RGYILE

Enzyme Prediction     

No EC number prediction in MGYG000000709_00010.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	161	462	3.3e-120	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	103	498	1	388	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	6.05e-105	98	528	116	560	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	2.87e-88	4	498	5	576	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
pfam00128	Alpha-amylase	1.82e-61	161	462	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	4.50e-58	104	497	1	399	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUC03509.1	1.16e-174	2	536	3	601
ADK68793.1	2.83e-164	4	539	5	601
ATP53560.1	2.53e-162	2	542	3	605
QIA33253.1	1.08e-160	2	542	3	605
SDS02076.1	4.41e-160	4	546	7	620

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1SMA_A	2.61e-86	98	545	129	555	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
1J0H_A	5.14e-86	98	545	129	555	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	1.42e-85	98	545	129	555	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	3.92e-85	98	545	129	555	Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.]
2Z1K_A	3.53e-79	100	525	3	421	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
P36905	1.35e-88	2	532	256	876	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P16950	1.48e-88	2	545	253	866	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38939	7.17e-88	2	545	253	865	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P38536	1.14e-87	2	545	256	865	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
A0A7U9P668	2.81e-85	98	545	129	555	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 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
1.000042	0.000011	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000709_00010.