CAZyme Information: MGYG000004764_01399

Basic Information

• Species: UBA2856 sp900555005
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA2856; UBA2856 sp900555005
• CAZyme ID: MGYG000004764_01399
• CAZy Family: GH13
• CAZyme Description: Neopullulanase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
292		33403.46	4.9444

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004764	1953582	MAG	China	Asia

• Gene Location: Start: 2167; End: 3045 Strand: +

Full Sequence      

MFRQAVRKANPDALILAEHYGSAWDWLLGDQWDSIMNYDAFMEPVSWFFTGMEKHSDEYL
PDQVGNADSFFGAMRYHTSNMMEPSLLTAMNELSNHDHSRFLTRTNHKVGRVGSFNYDAA
SDGVSCGVMRQAVLCQMTWPGAPTIYYGDEAGVCGFTDPDNRRTYPWGHENQEMIAYTRD
VIAMRRAHPVLRTGSLCYLHGERNCIAYARFDSRETVIVIFSIHPENMIVSLPVWQAETA
MECSVRRVFQTDEEGYSLEEKELEVSRGRLSLTLAPMSAEVFVYENHEGSYH

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	2	160	1.5e-33	0.4525316455696203

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	1.80e-67	2	196	222	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	7.18e-43	2	236	356	570	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	4.19e-21	1	195	357	576	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
pfam00128	Alpha-amylase	1.92e-10	2	159	195	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	1.09e-08	2	167	222	372	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRT48963.1	4.08e-114	2	281	395	674
QNM07495.1	4.86e-114	2	284	409	694
QRO37205.1	1.12e-110	2	279	395	672
QBF73915.1	1.12e-110	2	279	395	672
QYX27187.1	1.59e-110	2	279	395	672

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z0U_A	5.29e-35	2	236	369	587	Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) 11 residues (from A363 to N373) deletion mutant (Del11) [Thermoactinomyces vulgaris]
1IZJ_A	5.61e-35	2	236	380	598	ChainA, amylase [Thermoactinomyces vulgaris]
1JI1_A	5.61e-35	2	236	380	598	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]
2D0F_A	5.61e-35	2	236	380	598	ChainA, alpha-amylase I [Thermoactinomyces vulgaris]
5Z0T_A	5.61e-35	2	236	380	598	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q60053	3.50e-34	2	236	409	627	Neopullulanase 1 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaI PE=1 SV=1
Q59226	1.30e-27	2	222	338	533	Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
P38940	2.02e-27	2	233	341	547	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q08751	2.72e-27	2	276	338	575	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
P21517	9.93e-27	4	219	359	555	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
1.000059	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004764_01399.