dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003742_00485

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Basic Information help

Species

Prevotella buccalis

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella buccalis

CAZyme ID

MGYG000003742_00485

CAZy Family

GH13

CAZyme Description

Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
653	MGYG000003742_9\|CGC2	73833.27	6.2094

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003742	2540681	MAG	Canada	North America

Gene Location

Start: 49835; End: 51796 Strand: +

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.41	3.2.1.68	3.2.1.1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	185	509	5.4e-112	0.9965397923875432

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	151	552	2	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.
TIGR02104	pulA_typeI	0.0	37	626	16	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.
COG1523	PulA	2.70e-135	75	652	102	692	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	3.61e-112	35	612	130	855	alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. 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 is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102). [Energy metabolism, Biosynthesis and degradation of polysaccharides]
PLN02877	PLN02877	1.54e-105	58	610	238	924	alpha-amylase/limit dextrinase

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUB46864.1	3.46e-313	1	649	1	637
ALO49594.1	3.59e-313	37	649	30	638
AGB28439.1	4.79e-311	30	651	32	660
ATV55021.1	1.75e-305	23	649	17	635
ATV30616.1	4.07e-304	23	649	17	635

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	7.07e-171	37	610	45	619	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]
6JHH_A	1.13e-169	37	610	45	619	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	1.13e-169	37	610	45	619	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
2WAN_A	1.60e-144	37	651	322	921	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	1.12e-127	35	555	66	614	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	1.19e-128	37	616	229	812	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	9.88e-121	37	617	110	682	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	4.51e-67	58	640	231	941	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	1.73e-60	58	608	461	1076	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	1.79e-60	151	608	587	1091	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000417	0.995840	0.003149	0.000201	0.000183	0.000182

TMHMM Annotations download full data without filtering help

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