Glycoside Hydrolase Family 134

Activities in Familyendo-β-1,4-mannanase (EC 3.2.1.78);
Mechanism inverting
3D Structure Statuslysozyme fold
NoteCreated after the work by Shimizu and collaborators. J. Biol. Chem. (2015). [ PMID:26385921 ]. Presents an inverting mechanism in what is a unique feature compared to all other b-mannanases [see Jin et al. ACS Cent. Sci (2016) doi:10.1021/acscentsci.6b00232 ]
External resourcesCAZypedia;
Statistics GenBank accession (165); Uniprot accession (4); PDB accession (9); 3D entries (2); cryst (0)
Bacteria
Protein Name EC#ReferenceOrganismGenBank UniprotPDB/3D
 β-1,4-mannanase (SsGH134) 3.2.1.78 pubmed
Streptomyces sp. NRRL B-24484 WP_030268297.1 A0A1L1QK12
A0A1L1QK13
A0A1L1QK16
5JTS[A]
5JU9[A]
5JUG[A]
Eukaryota
Protein Name EC#ReferenceOrganismGenBank UniprotPDB/3D
 endo-β-1,4-mannanase (AN2710;ANID_02710) (Man134A) 3.2.1.78 pubmed
Aspergillus nidulans FGSC A4 EAA63112.1 A0A1U8QM87  
 AO090038000445 3.2.1.78 pubmed
Aspergillus oryzae RIB40 BAE64233.1    
 endo-β-1,4-mannanase (LpsGH134b) 3.2.1.78 pubmed
Lyrodus pedicellatus VAX65845.1    
 endo-β-1,4-mannanase (LpsGH134a) 3.2.1.78 pubmed
Lyrodus pedicellatus VAX65843.1    
 endo-β-1,4-mannanase (RMCBS344292_04886) 3.2.1.78 pubmed
Rhizopus microsporus CEI90564.1   5XTJ[A,B]
5XTT[A,B]
5XU5[A,B]
5XUG[A,B]
5XUL[A,B]
5XXA[A,B]
Top


Last update: 2022-06-09 © Copyright 1998-2022
AFMB - CNRS - Université d'Aix-Marseille