Activities in Family	Binding to maltotriose and maltotetraose shown for the pullulanase of Anoxybacillus sp. LM18-11. Binding function derived from crystal structure and deletion of the CBM, which showed reduced specific activity and increased Km value compared to the wild type enzyme.
Note	Family created following Xu et al., Proteins 82:1685-1693 [PMID: 24375572].
Statistics	GenBank accession (1286); Uniprot accession (10); PDB accession (6); 3D entries (2); cryst (0)

Bacteria
Protein Name	EC#	Organism	GenBank	Uniprot	PDB/3D Carbohydrate Ligands Resolution (Å)
pullulanase type I (PulA)		Anoxybacillus sp. LM18-11	AEW23439.1	K9L0H1	3WDH[A] 1.75 3WDI[A] α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp 2.20 3WDJ[A] α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp 2.22
pullulanase type I / glycogen-debranching enzyme (AmyX;BSU29930)		Bacillus subtilis subsp. subtilis str. 168	AAC00283.1 ACH14984.1 AIY94319.1 AQR83021.1 AQR87236.1 CAB14971.1 CAB14971.2 NP_390871.1	A0A6M4JN50 C0SPA0 O34587	2E8Y[A,B] 2.11 2E8Z[A,B] 2.20 2E9B[A,B] α-D-Glcp-(1-4)-α-D-Glcp α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp β-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp 2.30
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