| IED ID | IndEnz0011000005 |
| Enzyme Type ID | glucanase000005 |
| Protein Name |
Endo-1,3 4 -beta-glucanase 1 Endo-1,3-beta-glucanase 1 Endo-1,4-beta-glucanase 1 EC 3.2.1.6 Daughter specific expression protein 4 Laminarinase |
| Gene Name | ENG1 ACF3 DSE4 CAALFM_C103680WA CaO19.10584 CaO19.3066 |
| 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 | MLFKSVLLSTLIAVQALAENSAHQEIVTVTKTTHISNPCLENYAKKLLPNNPTGLTTGIPIVIVYAPQQPDNQVKQSESLQPTQSSKAQQQQQIQGSSVPASIHDTPTPTDHTKITVTSTTICNQKVCTVKTFSTIISHSESPTTTTTTKQNEEKSIADTKSFTHKALPSSNGAVTLKTTSVKTALTTTSTVFSATSLPSTTYTPSTSVSLVSTTKKNPVSSQSVVSTTKTISINTSLITDAVTITKEATTLPNSKHSSIFTNGSISFISTSANKVKSTVTSDISNNSQNGSSLSLTSTINQLASITNSTLTTITKPTSLVPDFSYTNSSRVSSTMRNSSEESSMVLEKSSSKLLSSTSFLNSSSIASTTESSELASATTSDSSLNHSSSSSVELSSSLSSEADSSSSSESVETGSSDETASNYSGDLFKAIDTNAPPTVFARSEIPLTIPAGVDNNGKPIGTNKFYTNLLLGNQDFMVYPLPYGLYWSKTSYYGFAVQHNNVSDRVFGSINTNNKGVASYYFNPTNNAELIFSATSFSKDSMHMKVSQMAELSALVTLSSSSNDESNYLDIPLVQGMGFVTGIYNGNLTPLLNSLFGVKDLSLETSDALLSNVLKYRATLLNNVQWLIYVTLPDKDTDFKLEVEDFYNLKGSKPVDGLIIQVAIAPEDNDNDKYYDAAAGMYVTGATVSGSVSQGTAASYKFSYTTAGKSSSNNPIVFALPHHMDSLTGSALDALTGITVTSTTKGEMTGFLTNELEFSETINQDVEFLPWTENMTGSLTYTKDQLELLASAANKELAANIAATVKNMNSNYFSGKVLDKYAQILLVVSEIIQDEEVTKDALNAMKDAFKVFTQNKQYYPLMYDTKFGGVTSTSAQDGDPNADFGSAYYNDHDFHYGYFIHAAAIVGYVDKKLGGTWAQSNKDWVNSLVRDASNPSADDTYFPVSRMFDWFSGHSWATGLFVTYKNIESSSESLHFAAAIKLWGKVVGDQSMEARGGLMISIMARSFNMYFYYKSDNTVEPKQILPNKVSGIFFENKVDYTTFFGTPADHPEYVHGIHMLPITPSSSLVRKTSYVQEEWKDQIAGFIDNVDSGWTGILRLNQALFDPKSSYEFFASNNWDDKWLDNGQSRTWSLAFAAGALNAS |
| Enzyme Length | 1145 |
| Uniprot Accession Number | Q5AIR7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6; Evidence={ECO:0000269|PubMed:16328626}; |
| DNA Binding | |
| EC Number | 3.2.1.6 |
| Enzyme Function | FUNCTION: Endo-1,3(4)-beta-glucanase involved in the cell separation process. Plays no essential role in growth, nor is it involved in hyphal morphogenesis. {ECO:0000269|PubMed:16328626}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (12); Region (3); Signal peptide (1) |
| Keywords | Cell wall;Glycoprotein;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is decreased during the hyphal transition, in biofilm, as well as by heat stress, caspofungin, fluconazole, and alpha pheromone. Transcription is also regulated by ACE2 and SIT4. {ECO:0000269|PubMed:14731272, ECO:0000269|PubMed:16328626, ECO:0000269|PubMed:16987174, ECO:0000269|PubMed:16998073, ECO:0000269|PubMed:19527170, ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:23136884, ECO:0000269|PubMed:23243062}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:23136884, ECO:0000269|PubMed:23243062}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 124,051 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |