| IED ID | IndEnz0008000370 |
| Enzyme Type ID | cellulase000370 |
| Protein Name |
Endoglycoceramidase I EGCase I EC 3.2.1.123 |
| Gene Name | REQ_38260 |
| Organism | Rhodococcus hoagii (strain 103S) (Rhodococcus equi) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Nocardiaceae Rhodococcus Rhodococcus hoagii (Corynebacterium equii) Rhodococcus hoagii (strain 103S) (Rhodococcus equi) |
| Enzyme Sequence | MRKTVVAFAAAIAACSAVLSSTTTSAAPPATPITTLQADGTHLVDGYGRTVLLHGVNNVDKDAPYLPAGETLTPQDIDILVRHGFNTVRLGTSFDALMPQRGQIDEAYLDRLTGVVDALTARGMHVLLDNHQDGLSKAWGGNGFPEWAIESRPREWEPNPGFPLYYLMPSLNAGWDEVWGNTHGALDHLGTALGALAERVEGKPGVMGIELLNEPWPGSRFLSCFPNGCPDFDRTYQAAMQKLTDAVRAQNPTIPVYWEPNVTWNQMMPSNLFAPPVTPALTTADVVFAPHDYCIPSQLAIYLGLPQALRGLCVPQQDLTWSNIDAITERANVPTVITEFGDGDPTVLKNTLARADERFIGWQYWHFGAGNATDPFLGEVGRQLVRTYPQATAGEPGRMIFDADNGDFAYRFTPRAATRPTEIFVSDLHYPDGYAVQVDGGQVTSAPGARIVTVVADGSGPVTVKINRPGSAGAEVPDGPIETSSSGSSGSS |
| Enzyme Length | 492 |
| Uniprot Accession Number | A0A3S5YBC7 |
| Absorption | |
| Active Site | ACT_SITE 214; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O85465; ACT_SITE 339; /note=Nucleophile; /evidence=ECO:0000305|PubMed:28179425 |
| Activity Regulation | |
| Binding Site | BINDING 61; /note="Substrate"; /evidence="ECO:0000269|PubMed:28179425, ECO:0007744|PDB:5J14, ECO:0007744|PDB:5J7Z"; BINDING 62; /note="Substrate"; /evidence="ECO:0000269|PubMed:28179425, ECO:0007744|PDB:5J7Z"; BINDING 265; /note="Substrate"; /evidence="ECO:0000269|PubMed:28179425, ECO:0007744|PDB:5J14, ECO:0007744|PDB:5J7Z"; BINDING 298; /note="Substrate"; /evidence="ECO:0000269|PubMed:28179425, ECO:0007744|PDB:5J14, ECO:0007744|PDB:5J7Z"; BINDING 302; /note="Substrate"; /evidence="ECO:0000269|PubMed:28179425, ECO:0007744|PDB:5J14, ECO:0007744|PDB:5J7Z"; BINDING 365; /note="Substrate"; /evidence="ECO:0000269|PubMed:28179425, ECO:0007744|PDB:5J14, ECO:0007744|PDB:5J7Z" |
| 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:28179425};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22289; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=ganglioside GM3 + H2O = an N-acyl-sphingoid base + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-D-glucose; Xref=Rhea:RHEA:65540, ChEBI:CHEBI:15377, ChEBI:CHEBI:79210, ChEBI:CHEBI:83273, ChEBI:CHEBI:156068; Evidence={ECO:0000269|PubMed:28179425};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65541; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=ganglioside GM1 + H2O = an N-acyl-sphingoid base + beta-D-Gal-(1->3)-beta-D-GalNAc-(1->4)-[alpha-Neu5Ac-(2->3)]-beta-D-Gal-(1->4)-D-Glc; Xref=Rhea:RHEA:65544, ChEBI:CHEBI:15377, ChEBI:CHEBI:82639, ChEBI:CHEBI:83273, ChEBI:CHEBI:156537; Evidence={ECO:0000269|PubMed:28179425};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65545; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=ganglioside Fuc-GM1 + H2O = alpha-Fuc-(1->2)-beta-Gal-(1->3)-beta-GalNAc-(1->4)-[alpha-Neu5Ac-(2->3)]-beta-Gal-(1->4)-Glc + an N-acyl-sphingoid base; Xref=Rhea:RHEA:65548, ChEBI:CHEBI:15377, ChEBI:CHEBI:83273, ChEBI:CHEBI:90189, ChEBI:CHEBI:156538; Evidence={ECO:0000269|PubMed:28179425};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65549; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H2O = an N-acyl-sphingoid base + lactose; Xref=Rhea:RHEA:65552, ChEBI:CHEBI:15377, ChEBI:CHEBI:17716, ChEBI:CHEBI:79208, ChEBI:CHEBI:83273; Evidence={ECO:0000269|PubMed:28179425};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65553; Evidence={ECO:0000269|PubMed:28179425}; |
| DNA Binding | |
| EC Number | 3.2.1.123 |
| Enzyme Function | FUNCTION: Hydrolyzes glycosphingolipids; exhibits broad substrate specificity including monosialodihexosylganglioside (GM3), monosialotetrahexosylganglioside (GM1), fucosyl-GM1, lactosylceramide, globotriosylceramide, globotetraosylceramide, ganglioside GD1a, and ganglioside GD1b (PubMed:28179425). No activity towards glucosylceramide and galactosylceramide (PubMed:28179425). {ECO:0000269|PubMed:28179425}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (21); Binding site (6); Chain (1); Disulfide bond (2); Helix (16); Lipidation (2); Mutagenesis (12); Region (3); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Disulfide bond;Glycosidase;Hydrolase;Lipid metabolism;Lipoprotein;Membrane;Palmitate;Secreted;Signal;Sphingolipid metabolism |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28179425}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..14; /evidence=ECO:0000255|PROSITE-ProRule:PRU00303 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 5CCU; 5J14; 5J7Z; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,830 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for monosialotetrahexosylganglioside (GM1) {ECO:0000269|PubMed:28179425}; Note=kcat is 10.5 sec(-1) with monosialotetrahexosylganglioside as substrate. {ECO:0000269|PubMed:28179425}; |
| Metal Binding | |
| Rhea ID | RHEA:22288; RHEA:22289; RHEA:65540; RHEA:65541; RHEA:65544; RHEA:65545; RHEA:65548; RHEA:65549; RHEA:65552; RHEA:65553 |
| Cross Reference Brenda | 3.2.1.123; |