P57965 · NUDC_PASMU
- ProteinNAD-capped RNA hydrolase NudC
- GenenudC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids264 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
Catalytic activity
- a 5'-end NAD+-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-nicotinamide D-ribonucleotide + 2 H+This reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Divalent metal cations. Mg2+ or Mn2+.
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 70 | substrate | |||
Binding site | 99 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 102 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 112 | substrate | |||
Binding site | 117 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 122 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 127 | substrate | |||
Binding site | 161 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 177 | a divalent metal cation 2 (UniProtKB | ChEBI) | |||
Binding site | 177 | a divalent metal cation 3 (UniProtKB | ChEBI) | |||
Binding site | 181 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 181 | a divalent metal cation 3 (UniProtKB | ChEBI) | |||
Binding site | 195-202 | substrate | |||
Binding site | 222 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 222 | a divalent metal cation 3 (UniProtKB | ChEBI) | |||
Binding site | 245 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | magnesium ion binding | |
Molecular Function | manganese ion binding | |
Molecular Function | NAD+ diphosphatase activity | |
Molecular Function | NADH pyrophosphatase activity | |
Molecular Function | RNA NAD-cap (NMN-forming) hydrolase activity | |
Molecular Function | zinc ion binding | |
Biological Process | NAD catabolic process | |
Biological Process | NADH metabolic process | |
Biological Process | NADP catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD-capped RNA hydrolase NudC
- EC number
- Short namesDeNADding enzyme NudC
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Pasteurella
Accessions
- Primary accessionP57965
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000056971 | 1-264 | NAD-capped RNA hydrolase NudC | ||
Interaction
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 128-252 | Nudix hydrolase | |||
Motif | 162-183 | Nudix box | |||
Sequence similarities
Belongs to the Nudix hydrolase family. NudC subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length264
- Mass (Da)29,767
- Last updated2001-04-27 v1
- Checksum52F8A97F348620B6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE004439 EMBL· GenBank· DDBJ | AAK03819.1 EMBL· GenBank· DDBJ | Genomic DNA |