Detail Information for IndEnz0011000143
IED ID IndEnz0011000143
Enzyme Type ID glucanase000143
Protein Name Mutanase Pc12g07500
EC 3.2.1.59
Endo-1,3-alpha-glucanase Pc12g07500
Glucan endo-1,3-alpha-glucosidas Pc12g07500
Gene Name PCH_Pc12g07500
Organism Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium chrysogenum species complex Penicillium rubens Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum)
Enzyme Sequence MIWKSLFSALAILTHILPALTAPALDSELSSQSEDKYVFAHFMVGIVKDYQLEDWKEDMTTAQSIGIDAFALNCASIDSYTPTQLALAYEAAEQVNFKVVISFDFAYWTNGDTEKITEYMKQYAGHPAQMQYKGAAVVSTFVGDSFNWDAVKQNTPHPIYAVPNLQDPAEATTGPAKSADGAFSWLAWPTDGGNSIIPGPMTTVWDDRFVHFLAGKTYMAPVSPWFSTHFNTKNWVFVCENLPTLRWEQMLSLQPDLIEIISWNDYGESHYIGPYSAHHSDDGSSQWATNMPHDGWRNLFKPYIAAYKSGAKTPTVEADEVVYWYRPTPKGVVCTGDTLSAPMGADMLSDSIFVATMLTSPGTLTVQSGNNAPVDIEVPAGIVTSNVTMGVGAQSFKVARDGQTILSGQGGLDVKDSCVHYNFNVYVGSTKGGDGSNTTGARGSM
Enzyme Length 445
Uniprot Accession Number B6GX22
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran.; EC=3.2.1.59; Evidence={ECO:0000269|PubMed:24884713};
DNA Binding
EC Number 3.2.1.59
Enzyme Function FUNCTION: Hydrolyzes 1,3-alpha-glucan predominantly into pentasaccharides. May enhance the efficacy of fungal antibiotics by degrading bacterial exopolysaccharides. {ECO:0000269|PubMed:24884713}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Glycosylation (2); Signal peptide (1)
Keywords Glycoprotein;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal
Interact With
Induction INDUCTION: Expression is induced in response to the presence of B.subtilis. {ECO:0000269|PubMed:24884713}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24884713}.
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 48,546
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.59;