dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000721_01524

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Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; NC2004;

CAZyme ID

MGYG000000721_01524

CAZy Family

CBM34

CAZyme Description

Neopullulanase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
702	MGYG000000721_15\|CGC1	81115.95	5.2031

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000721	2405891	MAG	Kazakhstan	Asia

Gene Location

Start: 37871; End: 39979 Strand: +

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	197	577	1.7e-98	0.9968354430379747
CBM34	44	137	3.5e-18	0.8833333333333333

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	2.05e-172	144	612	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	3.89e-142	49	655	18	572	maltodextrin glucosidase; Provisional
pfam00128	Alpha-amylase	1.21e-57	197	576	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	5.69e-52	145	652	1	495	Glycosidase [Carbohydrate transport and metabolism].
PRK14510	PRK14510	8.71e-45	54	612	25	576	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
QUF80610.1	9	701	8	700
CBK83607.1	13	699	7	694
SOB73560.1	9	702	10	703
QNL99521.1	15	700	10	695
BBF44784.1	1	700	1	699

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z0T_A	2.88e-122	30	699	10	635	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]
1JI1_A	4.43e-121	30	699	10	635	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]
1IZJ_A	6.24e-121	30	699	10	635	ChainA, amylase [Thermoactinomyces vulgaris]
1IZK_A	1.23e-120	30	699	10	635	ChainA, amylase [Thermoactinomyces vulgaris]
5Z0U_A	1.79e-120	30	699	10	624	Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) 11 residues (from A363 to N373) deletion mutant (Del11) [Thermoactinomyces vulgaris]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q60053	5.48e-120	30	699	39	664	Neopullulanase 1 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaI PE=1 SV=1
Q08341	8.96e-95	49	682	21	581	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P38939	7.08e-89	50	699	273	917	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
Q08751	3.35e-85	30	655	4	549	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
P16950	8.36e-84	50	627	273	846	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999873	0.000148	0.000006	0.000000	0.000000	0.000001

TMHMM Annotations help

There is no transmembrane helices in MGYG000000721_01524.