A0A4T1ZUW9 · A0A4T1ZUW9_9PSED
- ProteinNAD-capped RNA hydrolase NudC
- GenenudC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids275 (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
- NAD+ + H2O = beta-nicotinamide D-ribonucleotide + AMP + 2 H+
- 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 | 81 | substrate | |||
Binding site | 111 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 114 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 124 | substrate | |||
Binding site | 129 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 132 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 137 | substrate | |||
Binding site | 171 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 187 | a divalent metal cation 3 (UniProtKB | ChEBI) | |||
Binding site | 187 | a divalent metal cation 2 (UniProtKB | ChEBI) | |||
Binding site | 191 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 191 | a divalent metal cation 3 (UniProtKB | ChEBI) | |||
Binding site | 205-212 | substrate | |||
Binding site | 232 | a divalent metal cation 3 (UniProtKB | ChEBI) | |||
Binding site | 232 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 254 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A4T1ZUW9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 138-261 | Nudix hydrolase | |||
Motif | 172-193 | Nudix box | |||
Sequence similarities
Belongs to the Nudix hydrolase family. NudC subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length275
- Mass (Da)31,015
- Last updated2019-07-31 v1
- Checksum5051099A42DB561B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
RFLV01000002 EMBL· GenBank· DDBJ | TIH08085.1 EMBL· GenBank· DDBJ | Genomic DNA |