IED ID | IndEnz0008000232 |
Enzyme Type ID | cellulase000232 |
Protein Name |
Glucosylceramidase EC 3.2.1.45 Endoglycoceramidase-related protein 1 EGCrP1 Glucocerebrosidase |
Gene Name | ERC1 RO3G_04172 |
Organism | Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Mucoromycota Mucoromycotina Mucoromycetes Mucorales (pin molds) Mucorineae Rhizopodaceae Rhizopus Rhizopus delemar Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar) |
Enzyme Sequence | MTHPDRSAHDLNVPIQHSGRWFQDNLGRTLLLRGINVCGSSKLPTRPYPGSTHLYDDILFWDHRNVSFVNRPFPLEDAHEHFSRLSAWGLTLIRLLVPWESIEHEGPGCYDEEYIDYLRQLIEMMPRYGIKCIIDPHQDTWSRFSGGSGAPGWTFEVAGLNIKHFKETGAAYVHNTNAVPGDPLPMVWPTNYTKLASCTMFTLFFAGDTFAPHRTYQSQSIQQFLNHHFIEAYRHLAERLSDLEAVLAFEFMNEPHPGYIGLDHLDSFDPIMNLLFGDSPTPLQSFALGDGIPQTVDVYIKSWPFPTKKSHDRVINASQTSAWFSGCVWKEHGVWTVDDQGVPRLVNTHYFSKHPKTGEKISFYEDFYKPLVNRYVAAIQSVKKEYYCLVEPLANEKPPVYNEHDHHHNVIFSPHWYDLDSVFYKKFNARMTHDVQCLQRGGNVFSATYFGKRGAKKNYRGQIKNIKEDGLLNMGEKPCIMGEVGIPMDLNNKMAFEDDNYENHVHFMDAIIYALETNLISFTLWNYDVFNDHEYGDHWNGENFSIYSVKKSEEDYMRHDDGNSKLSKKHLYDGGRVLEAVLRPYAAKVAGTPVSAEFNIDTLQYTFSFIPDCKGSTTTEIFVPYFHYGNKTIKTDVSFGRCSYIEEFQTLYHQYELNDPLPKLVTITMGILTTESANSCSVM |
Enzyme Length | 683 |
Uniprot Accession Number | I1BTD7 |
Absorption | |
Active Site | ACT_SITE 254; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O85465; ACT_SITE 483; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O85465 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by metal cations Co(2+), Cu(2+), Ni(2+), Pb(2+) and Zn(2+) (PubMed:22072709). Not inhibited by metal chelator ethylenediaminetetraacetic acid (EDTA) (PubMed:22072709). {ECO:0000269|PubMed:22072709}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; EC=3.2.1.45; Evidence={ECO:0000269|PubMed:22072709};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270; Evidence={ECO:0000269|PubMed:22072709}; |
DNA Binding | |
EC Number | 3.2.1.45 |
Enzyme Function | FUNCTION: Specifically hydrolyzes the glucosidic linkage in glucosylceramide (PubMed:22072709). May prevent accumulation of aberrent glucosylceramide containing immature ceramide (By similarity). {ECO:0000250|UniProtKB:H1AE12, ECO:0000269|PubMed:22072709}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:22072709}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:22072709}; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Mutagenesis (2) |
Keywords | Glycosidase;Hydrolase;Membrane;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 78,542 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:13269; RHEA:13270 |
Cross Reference Brenda |