CAZyme Information: MGYG000002052_00144

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Stomatobaculum
• CAZyme ID: MGYG000002052_00144
• CAZy Family: GH13
• CAZyme Description: Neopullulanase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
684	MGYG000002052_9|CGC1	79168.02	6.0403

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002052	1357580	MAG	China	Asia

• Gene Location: Start: 8679; End: 10733 Strand: +

Full Sequence      

MERNAFFSDTSERFVTEWQTEGRTKIRVRFRGALNDKLRVSLILQEKKEETELLPVSGGR
RFRYYACTFSAEEAVSWLFLIEDRESGERLFYDRRGASTFARPELAFQHIPGFRTPEWAK
GAIMYQIFVDRFRNGGAENDVNTDEYIYIGLPVQHIENWDEKPSPFDVGYFYGGDLNGVR
EKFAYLKDLGVEVIYFNPLFVSPSNHKYDTQDYEHIDPHLTVIAEDGGEVLASDATDNLN
ATRYQKRSADPKNLAASDRFFAAFTEEAHRFGFRILLDGVFNHCGSFHKWLDREKIYAKQ
GSYAPGAYLERESPYHDYFVFMDDREKAWPDNRSYDGWWNNDTLPKLNYEASEELAERIL
RVGEKWLSPPYRVDGWRLDVAADLGHTQDYNHIFWKRFRARIKAVRRDALILAEHYGNPS
SWLNGREWDSVMNYDGFMEPVSWFLTGMEKHSDGKDPSLRGDGARFWDMMSLAIAKLPEP
SLHTAMNQLSNHDHSRFLTRTNGVVGRLAELGSAAAENGVQLSVMRQAALMLFTWPGAPT
LYYGDEVGVCGFTDPDSRRSYPWGHENLELLEYHRYLSKLHRNSQALRRGSLVPLLMERD
LVCYGRVYGREQVLIFVYTGEEDRLLRLPYWKLGDKLPQSVKRVMLTYEVGYNVGEVKYA
PEDGMILVYVTKNSAGIYLGTVKE

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	174	556	1.7e-84	0.9968354430379747

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	1.81e-154	121	592	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	2.65e-128	54	635	67	573	maltodextrin glucosidase; Provisional
pfam00128	Alpha-amylase	3.42e-51	174	555	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	5.47e-46	122	574	1	383	Glycosidase [Carbohydrate transport and metabolism].
cd11316	AmyAc_bac2_AmyA	7.56e-37	174	590	20	403	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
QUI96196.1	2.53e-287	1	678	1	677
QJU22212.1	1.26e-265	3	684	11	689
ASN93435.1	4.91e-265	3	684	11	689
QRP41905.1	4.91e-265	3	684	11	689
ADL06568.1	9.82e-265	1	675	8	679

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z0T_A	5.88e-91	62	670	74	627	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]
1IZJ_A	2.25e-90	62	670	74	627	ChainA, amylase [Thermoactinomyces vulgaris]
1JI1_A	3.15e-90	62	670	74	627	CrystalStructure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 [Thermoactinomyces vulgaris],1JI1_B Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 [Thermoactinomyces vulgaris],1UH3_A Thermoactinomyces vulgaris R-47 alpha-amylase/acarbose complex [Thermoactinomyces vulgaris]
5Z0U_A	3.37e-90	62	670	74	616	Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) 11 residues (from A363 to N373) deletion mutant (Del11) [Thermoactinomyces vulgaris]
1IZK_A	8.62e-90	62	670	74	627	ChainA, amylase [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q60053	3.45e-89	62	670	103	656	Neopullulanase 1 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaI PE=1 SV=1
P21517	4.98e-72	116	621	117	561	Maltodextrin glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=malZ PE=1 SV=5
P16950	1.14e-70	115	606	379	846	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38939	2.81e-70	115	668	379	918	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
Q08751	4.65e-69	24	667	21	581	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII 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
1.000018	0.000012	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002052_00144.