| IED ID | IndEnz0002015833 |
| Enzyme Type ID | protease015833 |
| Protein Name |
Peptide-N 4 - N-acetyl-beta-glucosaminyl asparagine amidase EC 3.5.1.52 Peptide:N-glycanase PNGase |
| Gene Name | png-1 F56G4.5 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MPVTEVGSLPELNNILERSDANRLIIIDFFANWCGPCRMISPIFEQFSAEYGNATFLKVNCDVARDIVQRYNISAMPTFIFLKNRQQVDMVRGANQQAIAEKIRQHYSPTPANPNAASDSEKRFLEQFVKCSNVPRSYQDEVFKALARSVMPEELVGRAMTEGPRDEKAILKDLLHWFKTQFFTWFDRPTCPKCTLKCSTDGLQGTPTREEQKEGGASRVEVYICDGCNTEMRFPRYNNPAKLLQTRTGRCGEWANCFGLLLAALNLESRFIYDTTDHVWNEVYLLAEQRWCHVDPCENTMDRPLLYTRGWGKTLGYCIGYGSDHVVDVTWRYIWDSKKLVTQRNEVRQPVFENFLSKLNSRQAEGQTEPRKRELAVRRVCELMEMMAQEAKNHKIGWEKIGDDLGGRITGSEEWRRERGELGESGPKLLAEPIKLAPPTGPAQNYLEFNYDVITDTYSQPPEIGFSAQAFELENVQRVEETDWNMTYLCRKRGDAPGNISWHFDLKSLKKSIEKIEIRMAGIQKFEKGKAMAIACLGDSCMRLPIDCSALTIEDPKNAEILKITATLSGGEGAIGFQQAQIFRTELKRGGGARTESFSVKIWMKN |
| Enzyme Length | 606 |
| Uniprot Accession Number | Q9TW67 |
| Absorption | |
| Active Site | ACT_SITE 251; /note=Nucleophile; ACT_SITE 278; /evidence=ECO:0000250; ACT_SITE 295; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Zn(2+) and z-VAD-fmk (caspase inhibitor) but unaffected by EDTA. {ECO:0000269|PubMed:17522090}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.; EC=3.5.1.52; |
| DNA Binding | |
| EC Number | 3.5.1.52 |
| Enzyme Function | FUNCTION: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation (PubMed:17509531, PubMed:17522090). Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp (PubMed:17522090). Prefers proteins containing high-mannose over those bearing complex type oligosaccharides (PubMed:17522090). Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins (PubMed:17509531). Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (PubMed:17509531). Also displays oxidoreductase (thioredoxin) activity (PubMed:17509531, PubMed:17522090). Involved in regulating the expression of proteasomal subunits such as rpt-3 in order to confer resistance to proteasomal dysfunction (PubMed:27528192). {ECO:0000269|PubMed:17509531, ECO:0000269|PubMed:17522090, ECO:0000269|PubMed:27528192}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (2); Metal binding (4); Mutagenesis (2) |
| Keywords | Cytoplasm;Endoplasmic reticulum;Hydrolase;Metal-binding;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17522090}. Endoplasmic reticulum {ECO:0000269|PubMed:17522090}. Note=ER localization inferred from partial colocalization with an ER marker, membrane protein PIG-X. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14704431; 15338614; 17850180; 19123269; 20130186; 20439776; 21085631; 21177967; 21367940; 22286215; 22560298; 23800452; 25487147; |
| Motif | |
| Gene Encoded By | |
| Mass | 69,148 |
| Kinetics | |
| Metal Binding | METAL 191; /note=Zinc; /evidence=ECO:0000250; METAL 194; /note=Zinc; /evidence=ECO:0000250; METAL 225; /note=Zinc; /evidence=ECO:0000250; METAL 228; /note=Zinc; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.5.1.52; |