IED ID | IndEnz0011000126 |
Enzyme Type ID | glucanase000126 |
Protein Name |
Endo-1,6-beta-D-glucanase neg1 EC 3.2.1.75 Beta-1,6-glucanase neg1 Glucan endo-1,6-beta-glucosidase neg1 |
Gene Name | neg1 AFUA_8G07120 |
Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Enzyme Sequence | MRISVGALLGLTALSHATTEKRAASASAYCSNSAGNYKLSSIAAPVQGAGNPGSESTWQLTVDDTSSGHKQTIVGFGAAVTDATVTSFNTLSASVLQDLLNKLMTPAGANFALMRHTIGASDLSGDPAYTYDDNGGKADPSLSGFNLGDRGTAMAKMLATMKSLQPNLKILGSPWSAPGWMKLNGVLDGNTNNNNLNDGYLTSGGTGSTGYASQFAQYFVKYIQAYKNLGAHVDAITIQNEPLFSSAGYPTMYVYDYESAQLIQNYIGPALASAGLDTEIWAYDHNTDVPSYPQTVLNQAGQYVKSVAWHCYAPNVDWTVLSQFHNTNPGVKQYMTECWTPASGAWHQAADFTMGPLQNWASGVAAWTLGTNAQDGPHLSTGGCATCQGLVTINNGGYTLNTAYYMMAQFSKFMPPGAIVLNGSGSYTYSGGGGIQSVASLNPDGTRTVVIENTFGNDVYVTVTMKSGQKWSGNAPSQSVTTWVLPSA |
Enzyme Length | 488 |
Uniprot Accession Number | Q4WBR2 |
Absorption | |
Active Site | ACT_SITE 241; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04062; ACT_SITE 337; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04062 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-glucans.; EC=3.2.1.75; Evidence={ECO:0000269|PubMed:19039584}; |
DNA Binding | |
EC Number | 3.2.1.75 |
Enzyme Function | FUNCTION: Endoglucanase that has highest activity on the linear beta-1,6-glucan pustulan and lower activity against laminarin (beta-1,3-glucans with beta-1,6-branches). Is active on C.albicans cell walls allowing the release of a previously described cell wall proteins. {ECO:0000269|PubMed:19039584}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:19039584}; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Glycosylation (1); Signal peptide (1) |
Keywords | Glycoprotein;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 51,430 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |