10.6084/m9.figshare.c.3621353_D1.v1 Johan Morrill Johan Morrill Evelina Kulcinskaja Evelina Kulcinskaja Anna Sulewska Anna Sulewska Sampo Lahtinen Sampo Lahtinen Henrik Stülbrand Henrik Stülbrand Birte Svensson Birte Svensson Maher Abou Hachem Maher Abou Hachem Additional file 13: of The GH5 1,4-β-mannanase from Bifidobacterium animalis subsp. lactis Bl-04 possesses a low-affinity mannan-binding module and highlights the diversity of mannanolytic enzymes Springer Nature 2015 Bifidobacterium Carbohydrate-binding module Gut microbiota Mannan Probiotic bacteria Surface plasmon resonance 2015-11-11 05:00:00 Figure https://springernature.figshare.com/articles/figure/Additional_file_13_of_The_GH5_1_4-_-mannanase_from_Bifidobacterium_animalis_subsp_lactis_Bl-04_possesses_a_low-affinity_mannan-binding_module_and_highlights_the_diversity_of_mannanolytic_enzymes/4394894 Multiple sequence alignment of characterized and predicted CBM10 sequences. The list of CBM10 sequences was obtained from the annotation software website dbCAN ( http://csbl.bmb.uga.edu/dbCAN/index.php ) with the exception of the SlMan5A CBM10 sequence which was added manually. The alignment was done with MAFFT 7 and rendered with ESPript 3. The positions corresponding to Cys5, Tyr8, Trp22, Trp24 and Cys36 in the CjXyn10A CBM10 structure [42] are indicated. The four cysteine residues form two disulphide bridges, while Tyr8, Trp22 and Trp24 where shown to mediate binding to insoluble cellulose in the CjXyn10A CBM10. (TIF 20792 kb)