IED ID | IndEnz0011000018 |
Enzyme Type ID | glucanase000018 |
Protein Name |
Glucan 1,3-beta-glucosidase I/II EC 3.2.1.58 Exo-1,3-beta-glucanase I/II Soluble cell wall protein 6 |
Gene Name | EXG1 BGL1 SCW6 YLR300W L8003.3 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Enzyme Sequence | MLSLKTLLCTLLTVSSVLATPVPARDPSSIQFVHEENKKRYYDYDHGSLGEPIRGVNIGGWLLLEPYITPSLFEAFRTNDDNDEGIPVDEYHFCQYLGKDLAKSRLQSHWSTFYQEQDFANIASQGFNLVRIPIGYWAFQTLDDDPYVSGLQESYLDQAIGWARNNSLKVWVDLHGAAGSQNGFDNSGLRDSYKFLEDSNLAVTTNVLNYILKKYSAEEYLDTVIGIELINEPLGPVLDMDKMKNDYLAPAYEYLRNNIKSDQVIIIHDAFQPYNYWDDFMTENDGYWGVTIDHHHYQVFASDQLERSIDEHIKVACEWGTGVLNESHWTVCGEFAAALTDCTKWLNSVGFGARYDGSWVNGDQTSSYIGSCANNDDIAYWSDERKENTRRYVEAQLDAFEMRGGWIIWCYKTESSLEWDAQRLMFNGLFPQPLTDRKYPNQCGTISN |
Enzyme Length | 448 |
Uniprot Accession Number | P23776 |
Absorption | |
Active Site | ACT_SITE 232; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 334; /note=Nucleophile; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; EC=3.2.1.58; |
DNA Binding | |
EC Number | 3.2.1.58 |
Enzyme Function | FUNCTION: Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme hydrolyzes both 1,3-beta- and 1,6-beta-linkages and even has beta-glucosidase activity. It could also function biosynthetically as a transglycosylase. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (10); Chain (1); Glycosylation (2); Helix (20); Propeptide (1); Sequence conflict (3); Signal peptide (1); Turn (4) |
Keywords | 3D-structure;Cell wall;Cell wall biogenesis/degradation;Cleavage on pair of basic residues;Direct protein sequencing;Glycoprotein;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9748433}. Secreted {ECO:0000269|PubMed:9748433}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1H4P; |
Mapped Pubmed ID | 10861899; 11471729; 11805837; 12209002; 12221112; 12237858; 12840001; 14690591; 14986091; 15256547; 15280361; 15834798; 16498706; 16760306; 19129178; 19536198; 21216897; 21267445; 21645823; 23135325; 23959528; 23991176; 24040173; 2532041; 26549048; 3033651; 3104142; 3111887; 7565410; 7565587; 7875558; 8298280; |
Motif | |
Gene Encoded By | |
Mass | 51,311 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |