| Known Activities | endo-α-N-acetylgalactosaminidase (EC 3.2.1.97) |
|---|---|
| Mechanism | Retaining |
| 3D Structure Status | ( β / α ) 8 |
| Catalytic Nucleophile/Base | Asp |
| Catalytic Proton Donor | Glu |
| Note | Created after Fujita et al. (2005) J. Biol. Chem. 280:37415-37422 (PMID: 16141207); catalytic residue determination : Willis et al. (2009) Biochemistry 48:10334-41 (PMID: 19788271) |
| External resources | CAZypedia; MEGAZYME; |
| Statistics | GenBank accession (96); Uniprot accession (46); PDB accession (2); 3D entries (3); cryst (1) |
| Bacteria | ||||||
| Protein Name | EC# | Organism | GenBank | Uniprot | PDB/3D | |
| core 1 endo-α-N-acetylgalactosaminidase (EngBF;BLLJ_0168) | 3.2.1.97 | Bifidobacterium longum subsp. longum JCM 1217 | AAX44931.1 BAJ65838.1 CAM83935.1 |
Q3T552 | 2ZXQ[A] | |
| endo-α-N-acetylgalactosaminidase (spr0328) (SpGH101) | 3.2.1.97 | Streptococcus pneumoniae R6 | AAK99132.1 CAM83936.1 |
Q8DR60 | 3ECQ[A,B] | |
| core 1 endo-α-N-acetylgalactosaminidase (EngSP;SP_0368) | 3.2.1.97 | Streptococcus pneumoniae TIGR4 | ABC75807.1 | cryst | ||