A0A719X2M0 · A0A719X2M0_SALTI
- ProteinNAD-capped RNA hydrolase NudC
- GenenudC
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids257 (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 | 69 | substrate | ||||
Sequence: R | ||||||
Binding site | 98 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 101 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 111 | substrate | ||||
Sequence: E | ||||||
Binding site | 116 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 119 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 124 | substrate | ||||
Sequence: Y | ||||||
Binding site | 158 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 174 | a divalent metal cation 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 174 | a divalent metal cation 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 178 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 178 | a divalent metal cation 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 192-199 | substrate | ||||
Sequence: QPWPFPQS | ||||||
Binding site | 219 | a divalent metal cation 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 219 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 241 | substrate | ||||
Sequence: A |
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 | 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 > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A719X2M0
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 125-248 | Nudix hydrolase | ||||
Sequence: PQIAPCIIVAIRREDSILLAQHVRHRNGVHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPQSLMTAFMAEYDSGEIVIDPKELLEANWYRYDDLPLLPPPGTVARRLIEDT | ||||||
Motif | 159-180 | Nudix box | ||||
Sequence: GFVEVGETLEQAVAREVMEESG |
Sequence similarities
Belongs to the Nudix hydrolase family. NudC subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length257
- Mass (Da)29,607
- Last updated2020-12-02 v1
- Checksum19B99052BD428C78