| IED ID | IndEnz0008000099 |
| Enzyme Type ID | cellulase000099 |
| Protein Name |
Endoglycoceramidase EGCase EC 3.2.1.123 Glycosphingolipid-specific enzyme GSL-specific enzyme |
| Gene Name | |
| Organism | Hydra vulgaris (Hydra) (Hydra attenuata) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Cnidaria Hydrozoa (hydrozoans) Hydroidolina Anthoathecata Aplanulata Hydridae (hydras) Hydra Hydra vulgaris (Hydra) (Hydra attenuata) |
| Enzyme Sequence | MISVALIILFLAKVISGKSDDFISVNPETNMLIDGYGRERFFHGTNVVVKHFPFHPETTGFNKDTFSEDDMKILQKFGLNSIRLGMMLPGYVPKREEYNETYIKVIQSIVTTAAKYGIYTLLDMHQDVFSPKFCVEGMPDWIVNTQGAKDFPMPLHKPFNLDPKTGYPYPEDCAKFSWADYYFTEAAGQAFQNLYDNVDGLRDEWAQFWKKTADVFKEEPSVIGYELINEPFCGNVFKHPTLLIPGVADYLNLQPTYDALQKAIRQVDEEHNIFFEGVTWDFFEVGFTEVPGGKQYQNRSVLSYHYYEPPDFSKKLNFEARLLDLKRLKCGGFLTEMFTVGTDFNSMFEMFDLCDKFKQSWHGWMYKSYGCIEQNLGCLNMSSPGKESIQIANTSRTYPQAVAGRTQSYAFDIKTKVFTLVYETVGSCKSGRTIVYFNKNLHYPNGYRYEINPNFKVTPSENEYFLYLDEVNKVPNTVVTFKLFPLSFTDSEDIHPVTVMGDKHLSENHNENEKKKK |
| Enzyme Length | 517 |
| Uniprot Accession Number | Q6L6S1 |
| Absorption | |
| Active Site | ACT_SITE 230; /note=Proton donor; /evidence=ECO:0000255 |
| Activity Regulation | ACTIVITY REGULATION: Cu(2+), zinc, manganese, calcium, magnesium and EDTA have no significant effects on enzyme activity. Enzyme requires presence of detergents such as Triton X-100 and Lubrol PX for the hydrolysis of glycosphingolipids. Taurodeoxycholate strongly inhibits the enzyme activity. {ECO:0000269|PubMed:15320336}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an oligoglycosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H2O = an N-acyl-sphingoid base + an oligoglycosyl-(1->4)-D-glucose; Xref=Rhea:RHEA:22288, ChEBI:CHEBI:15377, ChEBI:CHEBI:83273, ChEBI:CHEBI:136875, ChEBI:CHEBI:156536; EC=3.2.1.123; Evidence={ECO:0000269|PubMed:15320336}; |
| DNA Binding | |
| EC Number | 3.2.1.123 |
| Enzyme Function | FUNCTION: Hydrolysis of the glycosidic linkage between oligosaccharides and ceramides of glycosphingolipids, optimal substrates appear to be the glycosphingolipids with a gangliotetraose structure. {ECO:0000269|PubMed:15320336}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.0-4.0. Highly stable at acidic pH. {ECO:0000269|PubMed:15320336}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (4); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15320336}. Note=Released from digestive cells into the gastric cavity, and eventually into the surrounding medium, during the digestive process. {ECO:0000269|PubMed:15320336}. |
| 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 | 59,685 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:22288 |
| Cross Reference Brenda |