dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Lineage

Bacteria; Firmicutes; Bacilli; ML615J-28; CAG-313; UBA1737;

CAZyme ID

MGYG000000433_00722

CAZy Family

GH13

CAZyme Description

Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
675	MGYG000000433_15\|CGC1	79186.18	6.1174

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000433	1914532	MAG	Sweden	Europe

Gene Location

Start: 36306; End: 38333 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000000433_00722.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	238	545	5.2e-84	0.9965397923875432

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	2.16e-155	88	659	1	605	pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases.
cd11341	AmyAc_Pullulanase_LD-like	2.27e-143	204	588	1	406	Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. 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.
COG1523	PulA	8.26e-85	109	607	70	604	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02102	pullulan_Gpos	7.37e-61	111	608	332	912	pullulanase, extracellular, Gram-positive. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.
PLN02877	PLN02877	3.07e-55	98	606	214	869	alpha-amylase/limit dextrinase

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCV65359.1	1.34e-145	2	675	3	691
QMS84456.1	1.56e-134	4	675	5	698
AIO18683.1	2.42e-133	2	675	3	698
VEU82275.1	7.18e-132	6	675	3	648
CDR30743.1	2.80e-130	8	675	17	652

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WDH_A	3.10e-106	4	655	11	687	Crystalstructure of Pullulanase from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDI_A Crystal structure of Pullulanase complexed with maltotriose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDJ_A Crystal structure of Pullulanase complexed with maltotetraose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11]
2E8Y_A	2.30e-97	4	604	8	629	Crystalstructure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Y_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Z_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E8Z_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E9B_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis],2E9B_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis]
2WAN_A	4.69e-79	93	625	312	861	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
6JEQ_A	1.71e-75	94	602	36	572	Crystalstructure of Pullulanase from Paenibacillus barengoltzii complex with beta-cyclodextrin [Paenibacillus barengoltzii],6JFJ_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltohexaose and alpha-cyclodextrin [Paenibacillus barengoltzii],6JFX_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltopentaose [Paenibacillus barengoltzii],6JHF_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii],6JHG_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii in space group P212121 [Paenibacillus barengoltzii]
6JHI_A	2.38e-74	94	602	36	572	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C0SPA0	9.01e-97	4	604	8	629	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
O33840	5.96e-85	19	666	144	829	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
A0A0H2UNG0	6.35e-46	152	608	521	1048	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	2.01e-45	152	608	506	1033	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	2.74e-45	152	608	528	1055	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA 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
0.999922	0.000117	0.000013	0.000001	0.000000	0.000007

TMHMM Annotations help

There is no transmembrane helices in MGYG000000433_00722.

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