CAZyme Information: MGYG000000922_02298

Basic Information

• Species: UMGS416 sp900542005
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; UMGS416; UMGS416; UMGS416 sp900542005
• CAZyme ID: MGYG000000922_02298
• CAZy Family: GH13
• CAZyme Description: Amylopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
613	MGYG000000922_41|CGC1	69918.53	5.3817

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000922	2901170	MAG	China	Asia

• Gene Location: Start: 16244; End: 18085 Strand: +

Full Sequence      

MTLTIDAMDEPDAQIVLRRHSEAHGTEMIHGSPMPIPSGERWRFELTAPVDPGLFWYDFE
IHHQGQVRWYTAPDDGLGGEGAINAHTGKAWQVTVYQPVEGPLWPSQGIMYQIYVDRFYN
GYGDKRIEHAPDGALLHAHWEDTPFYTRDDRNAVVRWDFFGGNLKGVEEKLDYLQQMGVS
ILYLNPIFLSGSNHKYDTADYRRIDPMYGGEEAFASLMRAVRARGMRLILDGVFSHTGSD
SLYFNRQGRYGSLGAYQSQQSPYFSWYRFSNWPGQYDCWWGVETMPNVNELDPGYLAYQL
HDPDSTVRKWMGYGIDGFRLDVADELPDAFIAQLKDVIRQEKADSFLLGEVWEDASNKVS
YDVRRQYFMGRELDSVTNYPLRNALLELILGRRSPAAMVRLMKSLQENYPRAQFYSLMNM
TGTHDTPRLMTLLGEAPDPGTLTELERAQYRLSKGRRAMGQRRVGLYAAVLFTHPGIPTV
YYGDEAGMEGYADPYNRGPYPWGREDGEVQATFRRLSLLRRDEPLLSSGSYSPFALEGGL
YGHWRWQGNEGILTVINPGEDECVSRLPLSGHPVPEALWQVAGGSSWLQPEESGFRLHLA
GWDYLIVKVRAAR

Enzyme Prediction     

No EC number prediction in MGYG000000922_02298.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	162	494	1.1e-122	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	1.73e-179	107	531	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.
PRK14510	PRK14510	2.75e-101	37	532	44	578	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
PRK10785	PRK10785	7.34e-98	40	586	61	585	maltodextrin glucosidase; Provisional
cd11316	AmyAc_bac2_AmyA	1.69e-54	162	512	20	358	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.
cd11337	AmyAc_CMD_like	1.46e-48	144	531	14	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNB44994.1	1.37e-181	10	545	37	576
ATW28215.1	3.78e-179	45	545	74	575
AGA69642.1	1.88e-178	32	557	63	588
ARD65330.1	1.99e-178	34	557	53	575
ADO38823.1	7.99e-178	34	557	53	575

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5BN7_A	1.39e-67	1	584	24	585	Crystalstructure of maltodextrin glucosidase from E.coli at 3.7 A resolution [Escherichia coli K-12]
5Z0U_A	2.36e-67	24	582	59	589	Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) 11 residues (from A363 to N373) deletion mutant (Del11) [Thermoactinomyces vulgaris]
5Z0T_A	7.80e-66	24	582	59	600	Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE) [Thermoactinomyces vulgaris],5Z0T_B Thermoactinomyces vulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE) [Thermoactinomyces vulgaris]
2Z1K_A	2.41e-65	104	571	3	435	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]
1IZJ_A	1.07e-64	24	582	59	600	ChainA, amylase [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P36905	2.27e-96	37	541	316	842	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P16950	2.49e-95	37	545	313	846	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38536	6.32e-95	37	541	316	841	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P38939	9.02e-95	37	564	313	875	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P21517	5.97e-67	1	584	22	583	Maltodextrin glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=malZ PE=1 SV=5

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
1.000067	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000922_02298.