Detail Information for IndEnz0011000261
IED ID IndEnz0011000261
Enzyme Type ID glucanase000261
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 ACLA_064000
Organism Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
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 clavatus Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Enzyme Sequence MQTRQLLALALAVAATEAAHQGFNYGNTKSDGSAKSQSDFAAEFSTAKNLVGTSGFTSARLYTMIQGGTSATPISAIPAAIAEDTSLLLGIWASGGNVANEIAALKAAIAQYGADFGKHVVGISVGSEDLYRNSVDGVKSKAGLGANPDDLVSYIHQVREAIAGTSLSGAPIGHVDTWTAWVNGSNSAVIDACDWLGFDGYPYFQNTMPNSISDAKALFDESVAKTQAVAKGKEVWITETGWPVSGKTENLAVANTANAKAYWDQVGCPLFGNTNTWWYILQDADPVTPNPSFGIVGSTLSTTPLFDLSCSAVSSSSAVPSATAAATAASGAGASGSQTSGFATAAAGSSSAAKPTFSVGKGPNGSYNGTYPGSWNSTRPGANGGSSGSSGSSGSSGSSGSSGSSGSGASGHSSSTGSSSFPSSTNLLSNSASGLSGSLFGAVAAVFVALAAL
Enzyme Length 453
Uniprot Accession Number A1CD22
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 (4); 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 45,031
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda