IED ID | IndEnz0011000261 |
Enzyme Type ID | glucanase000261 |
Protein Name |
Probable glucan endo-1,3-beta-glucosidase eglC EC 3.2.1.39 Endo-1,3-beta-glucanase eglC Laminarinase eglC |
Gene Name | eglC ACLA_064000 |
Organism | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus clavatus Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
Enzyme Sequence | MQTRQLLALALAVAATEAAHQGFNYGNTKSDGSAKSQSDFAAEFSTAKNLVGTSGFTSARLYTMIQGGTSATPISAIPAAIAEDTSLLLGIWASGGNVANEIAALKAAIAQYGADFGKHVVGISVGSEDLYRNSVDGVKSKAGLGANPDDLVSYIHQVREAIAGTSLSGAPIGHVDTWTAWVNGSNSAVIDACDWLGFDGYPYFQNTMPNSISDAKALFDESVAKTQAVAKGKEVWITETGWPVSGKTENLAVANTANAKAYWDQVGCPLFGNTNTWWYILQDADPVTPNPSFGIVGSTLSTTPLFDLSCSAVSSSSAVPSATAAATAASGAGASGSQTSGFATAAAGSSSAAKPTFSVGKGPNGSYNGTYPGSWNSTRPGANGGSSGSSGSSGSSGSSGSSGSSGSGASGHSSSTGSSSFPSSTNLLSNSASGLSGSLFGAVAAVFVALAAL |
Enzyme Length | 453 |
Uniprot Accession Number | A1CD22 |
Absorption | |
Active Site | ACT_SITE 128; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O22317; ACT_SITE 239; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O22317 |
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: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Glycosylation (4); Lipidation (1); Propeptide (1); Region (1); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Cell membrane;Cell wall;Cell wall biogenesis/degradation;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Polysaccharide degradation;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}. Note=Covalently-linked GPI-modified cell wall protein. {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity). {ECO:0000250}. |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 45,031 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |