| IED ID | IndEnz0011000136 |
| Enzyme Type ID | glucanase000136 |
| Protein Name |
Probable endo-1,3 4 -beta-glucanase AFUA_2G14360 EC 3.2.1.6 Mixed-linked glucanase AFUA_2G14360 |
| Gene Name | AFUA_2G14360 |
| 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 | MAPSSLLLSVGSLITSSLVSATALEARQSQTYQLAESWQGESFINDWNFFDGADPTNGYVTYVNQSFAKQSGLVKVTESGSFYMGVDYESTLNPNGAGRESVRIESKNYYTEGLYVIDIEHMPGSICGTWPAFWSVGKNWPNDGEIDIIEGVNLQKANKIVLHTSGSCDVSGSNDMTGTLSSSECGEASGTVGCVVKGTNGSSGDPFNESGGGVYAMEWTDTFIKIWFFPRSQIPASLASGNPDTSSFGTPMAHLQGSCDFAERFKAQKLIIDTTFCGDWAGNVFAESTCPMSDPSSPMQSCVNYVAQNPAAFKEAYWEINSIKIYQYGVSAASSAAVSQATASKVEGTRVSAQAANTATPTVPAPVETTTVPQPAQTNTVATSAADHATPSSAETTTVPAATGAPSVSATEGGDSELESTSTVYVTSTTTICPVAESSSAAAAGGKEDAPSNGTSGAEVAATSVAAAAPAAATSGHPGADAIANSAAATSTDAQSESATSRLTAGALSEIPTAPPEPVSQAVSTGSFDDSDTAQGDSEEQGSIASASVAPSTIPVPASSSAAALGGSSIASSFASSRLIPRPTGSSTAASATAIATWSPTAGESASGTAKESATLTTPSEVFFTPGLSNGANRMSVGLSGLIGVMFIAALA |
| Enzyme Length | 652 |
| Uniprot Accession Number | Q4X084 |
| 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 (1); Domain (1); Glycosylation (4); 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 | 65,993 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.6; |