| IED ID | IndEnz0011000091 |
| Enzyme Type ID | glucanase000091 |
| 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 AN7950 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MFTKTQILALALSIASAEAVSKGFNYGANKPDGTLKVQADFEAEFRTAKNLETTSGFNSARLYTMIQGTGSTPISAIPAAIAEETTLLLGLWASGGNMDNEIAALKAAINQYGDEFAKLVVGISVGSEDLYRNSEIGVQANAGIGIEPEELVSYIQRVREAIAGTALSGAPIGHVDTWNAWTNGSNAAVAEAVDWLGFDGYPFFQNTMQNSIDDAKALFDESVQKTKAVAGNKEVWITETGWPVSGDSQNLAIASVENAKQFWDEVGCPLFDNVNTWWYILQDASGSSVPNPSFGIVGNTLSTTPLFDLSCSASSKKNSSSASASASGSSAQSTGFVSTTKPAASPSGSSGLGHGGSLGSSGSFSGGHYAGVGSSSVIASPSATPSGSAVPGSSSGPGSSSGSASGSSSGFGSGAAADSTSGTSTSGDSTSSTSATPADFTGAGSRLSGSIFGAAMLVAALAVAL |
| Enzyme Length | 465 |
| Uniprot Accession Number | Q5AUT0 |
| 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. {ECO:0000269|PubMed:15950156}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Glycosylation (2); Lipidation (1); Propeptide (1); Region (2); 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 | INDUCTION: Expression is under the control of the nsdD transcription factor required for sexual development. Transcript level is the highest at the beginning of asexual development and decreases thereafter to increase again at the late stage. {ECO:0000269|PubMed:15950156}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19585695}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:19585695}. Secreted, cell wall {ECO:0000269|PubMed:19585695}. Secreted {ECO:0000269|PubMed:25043916}. Note=Covalently-linked GPI-modified cell wall protein. |
| 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..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,685 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |