IED ID | IndEnz0011000281 |
Enzyme Type ID | glucanase000281 |
Protein Name |
Probable endo-1,3 4 -beta-glucanase NFIA_089530 EC 3.2.1.6 Mixed-linked glucanase NFIA_089530 |
Gene Name | NFIA_089530 |
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 | MAPSSLFLSVGSLIASSLVSATALEARQSQTYQLAESWQGESFINDWNFFDRADPTNGYVTYVNQSFAEQSGLVKVTQSGSFYMGVDYESTLNPNGPGRESVRIETKNYYTEGLYVIDIEHMPGSICGTWPAFWSVGKDWPNDGEIDIIEGVNLQKANKIVLHTSGSCDVSGSNDMTGTLSSSECGEASGTVGCVVKGTNGSSGDPFNEAGGGVYAMEWTDTFIKIWFFPRSQIPASLSSGNPDTSSFGTPMAHLQGSCDFAERFKAQKFIIDTTFCGDWAGNVFAESTCPMSDPSSPMQSCVNYVAQNPAAFKEAYWEINSIKVYQYGVSAASSAAVSQATASKVEGTLVSVQAANTATPTVPVPAETTAVPQPAQTNTVATSAADYATQSSAETTTVPAATGAPSVSAAEGGDSELESTSTVYVTSTTTICPVAESSSAAAAGGKKDAPFNGVSGAEVAATSVAAAPAAATSEHPGADAIANSAAATSTVAKSEGVASQLTAGALSEIPTAPPEPVSQAVSTGSFDDSDTAQGDSEEHGSIASASAAPSTIPVPASSSAAALGGSSIASSFASSRLVPRPTGSSTAASVTAIATWSPTAGERASGTAKGSATLTAPSEVVFTPGLSNGANRMSVGLSGLIGVMFIAALA |
Enzyme Length | 651 |
Uniprot Accession Number | A1DHY9 |
Absorption | |
Active Site | ACT_SITE 145; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 150; /note=Proton donor; /evidence=ECO:0000250 |
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; |
DNA Binding | |
EC Number | 3.2.1.6 |
Enzyme Function | FUNCTION: Mixed-linked glucanase involved in the degradation of complex natural cellulosic substrates. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Compositional bias (2); Domain (1); Glycosylation (2); Lipidation (1); Propeptide (1); Region (2); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Cell membrane;Cellulose degradation;GPI-anchor;Glycoprotein;Glycosidase;Hydrolase;Lipoprotein;Membrane;Polysaccharide degradation;Reference proteome;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 66,035 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |