Activities in Family	[retaining] reducing end exo-β-mannosidase (EC 3.2.1.-); β-mannosidase (EC 3.2.1.25); Endo-β-1,4-mannanase (EC 3.2.1.78);
Mechanism	Retaining e
Clan	GH-A
3D Structure Status	( β / α ) 8 barrel
Catalytic Nucleophile/Base	Glu (experimental)
Catalytic Proton Donor	Glu (experimental)
Note	Created based on Zhang et al. (2008) J. Biol. Chem. 283, 31551-31558 (PMID:18755688)
External resources	CAZypedia;
Statistics	GenBank accession (1976); Uniprot accession (19); PDB accession (14); 3D entries (3); cryst (0)

Bacteria
Protein Name	EC#	Organism	GenBank	Uniprot	PDB/3D Carbohydrate Ligands Resolution (Å)
endo-β-1,4-mannanase (ManA; AaManA; AaMan113A)	3.2.1.78	Alicyclobacillus acidocaldarius TC-12-31	ABG77968.1	A5H1I6	3CIV[A] 1.90 4CD6[A] <carb_like_IFM> 1.64 4CD7[A,B] β-D-Manp-(1-1)-<non_carb> β-D-Manp-(1-4)-α-D-Manp <carb_like_IFM> 1.65 4CD8[A] β-D-Manp <carb_like_MVL> 1.47
β-1,4-mannanase (AxMan113A)	3.2.1.78	Amphibacillus xylanus NBRC 15112	BAM48369.1	K0J0N5	5YLH[A,B] 2.29 5YLI[A,B] β-D-Manp-(1-4)-β-D-Manp-(1-4)-β-D-Manp-(1-4)-β-D-Manp 2.37 5YLK[A,B] β-D-Manp β-D-Manp-(1-4)-β-D-Manp 2.09 5YLL[A,B] β-D-Manp-(1-4)-β-D-Manp-(1-4)-β-D-Manp 1.81 5Z4T[A,B] β-D-Manp-(1-4)-β-D-Manp 1.68
endo-β-1,4-mannanase (ManB; BaMan113A) (Man113A)	3.2.1.78	Bacillus sp. N16-5	AML27062.1	A0A140EH91	7DV7[A,B] 1.44 7DVJ[A,B] β-D-Manp-(1-4)-β-D-Manp 1.65 7DVZ[A,B] 2.00 7DW8[A,B] β-D-Manp-(1-4)-β-D-Manp 1.90 7DWA[A,B] β-D-Manp-(1-4)-β-D-Manp-(1-4)-α-D-Manp 1.62
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