| IED ID | IndEnz0011000008 |
| Enzyme Type ID | glucanase000008 |
| Protein Name |
Glucan 1,3-beta-glucosidase EC 2.4.1.- EC 3.2.1.58 Exo-1,3-beta-glucanase |
| Gene Name | XOG1 EXG EXG1 XOG CAALFM_C102990CA Ca49C10.05 CaO19.10507 CaO19.2990 |
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Enzyme Sequence | MQLSFILTSSVFILLLEFVKASVISNPFKPNGNLKFKRGGGHNVAWDYDNNVIRGVNLGGWFVLEPYMTPSLFEPFQNGNDQSGVPVDEYHWTQTLGKEAASRILQKHWSTWITEQDFKQISNLGLNFVRIPIGYWAFQLLDNDPYVQGQVQYLEKALGWARKNNIRVWIDLHGAPGSQNGFDNSGLRDSYNFQNGDNTQVTLNVLNTIFKKYGGNEYSDVVIGIELLNEPLGPVLNMDKLKQFFLDGYNSLRQTGSVTPVIIHDAFQVFGYWNNFLTVAEGQWNVVVDHHHYQVFSGGELSRNINDHISVACNWGWDAKKESHWNVAGEWSAALTDCAKWLNGVNRGARYEGAYDNAPYIGSCQPMLDISQWSDEHKTDTRRYIEAQLDAFEYTGGWVFWSWKTENAPEWSFQTLTYNGLFPQPVTDRQFPNQCGFH |
| Enzyme Length | 438 |
| Uniprot Accession Number | P29717 |
| Absorption | |
| Active Site | ACT_SITE 230; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O85465; ACT_SITE 330; /note=Nucleophile; /evidence=ECO:0000269|PubMed:9013549 |
| Activity Regulation | ACTIVITY REGULATION: Binding of human antimicrobial peptide LL-37 decreases the catalytic activity, which leads to the decrease of cell adhesion. {ECO:0000269|PubMed:21713010}. |
| Binding Site | BINDING 65; /note=Substrate; /evidence=ECO:0000269|PubMed:20875088; BINDING 67; /note=Substrate; /evidence=ECO:0000269|PubMed:20875088; BINDING 230; /note=Substrate; /evidence=ECO:0000269|PubMed:20875088; BINDING 293; /note=Substrate; /evidence=ECO:0000269|PubMed:20875088; BINDING 300; /note=Substrate; /evidence=ECO:0000269|PubMed:20875088 |
| 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; Evidence={ECO:0000269|PubMed:10469155, ECO:0000269|PubMed:20875088, ECO:0000269|PubMed:21713010}; |
| DNA Binding | |
| EC Number | 2.4.1.-; 3.2.1.58 |
| Enzyme Function | FUNCTION: Major glucan 1,3-beta-glucosidase required for cell wall integrity. Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Can also function biosynthetically as a transglycosylase. Functions to deliver glucan from the cell to the extracellular matrix. Does not appear to impact cell wall glucan content of biofilm cells, nor is it necessary for filamentation or biofilm formation. Involved in cell-substrate and cell-cell adhesion. Adhesion to host-cell surfaces is the first critical step during mucosal infection. XOG1 is target of human antimicrobial peptide LL-37 for inhibition of cell adhesion. {ECO:0000269|PubMed:21713010, ECO:0000269|PubMed:22876186}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (10); Binding site (5); Chain (1); Disulfide bond (2); Helix (19); Mutagenesis (6); Propeptide (1); Sequence conflict (2); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Cell adhesion;Cell wall;Cell wall biogenesis/degradation;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal;Transferase;Virulence;Zymogen |
| Interact With | |
| Induction | INDUCTION: Expression is maximal during the early rapid growth phase and increases during biofilm growth. Induced by caspofungin. Transcripts is also regulated by RCK2, SIT4, and HTG4. {ECO:0000269|PubMed:14731272, ECO:0000269|PubMed:17030998, ECO:0000269|PubMed:20392151, ECO:0000269|PubMed:20402792, ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:22876186}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:1789004, ECO:0000269|PubMed:19555771, ECO:0000269|PubMed:20167299, ECO:0000269|PubMed:20641015, ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:23136884, ECO:0000269|PubMed:23243062}. Note=Is non-covalently attached to the cell wall. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /note=Or 25; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (12) |
| Cross Reference PDB | 1CZ1; 1EQC; 1EQP; 2PB1; 2PBO; 2PC8; 2PF0; 3N9K; 3O6A; 4M80; 4M81; 4M82; |
| Mapped Pubmed ID | 11112513; 24804868; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,056 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23.0 mM for laminaribiose {ECO:0000269|PubMed:10469155}; KM=12.7 mM for laminaritriose {ECO:0000269|PubMed:10469155}; KM=5.0 mM for laminaritetraose {ECO:0000269|PubMed:10469155}; KM=2.6 mM for laminaripentaose {ECO:0000269|PubMed:10469155}; KM=2.7 mM for laminarihexaose {ECO:0000269|PubMed:10469155}; KM=2.4 mM for laminariheptaose {ECO:0000269|PubMed:10469155}; KM=3.9 mM for laminarin {ECO:0000269|PubMed:10469155}; KM=17.9 mM for pustulan {ECO:0000269|PubMed:10469155}; KM=260 mM for gentiobiose {ECO:0000269|PubMed:10469155}; KM=120 mM for gentiotriose {ECO:0000269|PubMed:10469155}; KM=70 mM for cellobiose {ECO:0000269|PubMed:10469155}; KM=9.4 mM for cellotetraose {ECO:0000269|PubMed:10469155}; KM=12.0 mM for cellohexaose {ECO:0000269|PubMed:10469155}; KM=2.4 mM for p-nitrophenyl-beta-glucoside (pNPG) {ECO:0000269|PubMed:10469155}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.58; |