IED ID | IndEnz0011000084 |
Enzyme Type ID | glucanase000084 |
Protein Name |
Glucan endo-1,3-beta-glucosidase EC 3.2.1.39 1- 3 -beta-glucan endohydrolase 1- 3 -beta-glucanase |
Gene Name | |
Organism | Cellulosimicrobium cellulans (Arthrobacter luteus) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Promicromonosporaceae Cellulosimicrobium Cellulosimicrobium cellulans (Arthrobacter luteus) |
Enzyme Sequence | MPHDRKNSSRRAWAALCAAVLAVSGALVGVAAPASAVPATIPLTITNDSGRGPIYLYVLGERDGVAGWADAGGTFHPWPGGVGPVPVPAPDASIAGPGPGQSVTIRLPKLSGRVYYSYGQKMTFQIVLDGRLVQPAVQNDSDPNRNILFNWTEYTLNDGGLWINSTQVDHWSAPYQVGVQRADGQVLSTGMLKPNGYEAFYTALEGAGWGGLVQRAPDGSRLRALNPSHGIDVGKISSASIDSYVTEVWNSYRTRDMVVTPFSHEPGTQFRGRVDGDWFRFRSGSGQEVAAFKKPDASSVYGCHKDLQAPNDHVVGPIARTLCAALVRTTALTNPNQPDANSAGFYQDARTNVYAKLAHQQMANGKAYAFAFDDVGAHESLVHDGNPQAAYIKLDPFTGTATPLGNGGSTEQPGTPGGLPAGTGALRIGSTLCLDVPWADPTDTNQVQLATCSGNAAQQWTRGTDGTVRALGKCLDVARSGTADGTAVWIYTCNGTGAQKWTYDSATKALRNPQSGKCLDAQGGAPLRDGQKVQLWTCNQTEAQRWTL |
Enzyme Length | 548 |
Uniprot Accession Number | P22222 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; |
DNA Binding | |
EC Number | 3.2.1.39 |
Enzyme Function | FUNCTION: Lysis of cellular walls containing beta-1,3-glucans. Implicated in the defense against fungal pathogens. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Domain (1); Region (2); Signal peptide (1) |
Keywords | Cell wall biogenesis/degradation;Direct protein sequencing;Glycosidase;Hydrolase;Lectin;Periplasm;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1985933}. |
Modified Residue | |
Post Translational Modification | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. |
Signal Peptide | SIGNAL 1..36; /note="Tat-type signal"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000269|PubMed:1985933" |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 58,089 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.39; |