| IED ID | IndEnz0011000186 |
| Enzyme Type ID | glucanase000186 |
| 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 NFIA_000800 |
| Organism | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| 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 fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| Enzyme Sequence | MQFTQLVALALALATSEAAHQGFNYGNTKSDGSAKSQSDFQAEFSTAKNLVGTSGFTSARLYTMIQGGTANTPISAIPAAVAEETSLLLGLWASGGNFANEIAALKTAIADYGDDLAKLVVGISVGSEDLYRNSVDGVKAKAGLGTNPDEIVSYINQVRSTIAGTKLSGAPIGHVDTWTAWVNGSNSAVIDACDWLGFDGYPYFQNTMANSISDAKALFDESVAKTEAVAKGKEVWITETGWPVSGNTENLAVANLANAKTYWDEVGCPLFGKTNTWWYILQDANPVTPNPSFGIVGSTLSTTPLFDLSCSASSSAAASSTAVPSASSVAGAKASGFATAAASSGAAGSAKPTFTVGKGPGGSYNGTGFWNSTSSARPSSTAISGSSSGSASGSSGSSGSGASGASGQSSSSTGSSSAPSSSNILSNAASGLSGSIFGAVVAVCLALAAL |
| Enzyme Length | 450 |
| Uniprot Accession Number | A1DJ47 |
| 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 (3); 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 | 44,878 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |