A0AAE3RN80 · A0AAE3RN80_9ENTR

  • Protein
    NAD-capped RNA hydrolase NudC
  • Gene
    nudC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Divalent metal cations. Mg2+ or Mn2+.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site69substrate
Binding site98Zn2+ (UniProtKB | ChEBI)
Binding site101Zn2+ (UniProtKB | ChEBI)
Binding site111substrate
Binding site116Zn2+ (UniProtKB | ChEBI)
Binding site119Zn2+ (UniProtKB | ChEBI)
Binding site124substrate
Binding site158a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site174a divalent metal cation 2 (UniProtKB | ChEBI)
Binding site174a divalent metal cation 3 (UniProtKB | ChEBI)
Binding site178a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site178a divalent metal cation 3 (UniProtKB | ChEBI)
Binding site192-199substrate
Binding site219a divalent metal cation 3 (UniProtKB | ChEBI)
Binding site219a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site241substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular FunctionNAD+ diphosphatase activity
Molecular FunctionNADH pyrophosphatase activity
Molecular Functionzinc ion binding
Biological ProcessNAD catabolic process
Biological ProcessNADH metabolic process
Biological ProcessNADP catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NAD-capped RNA hydrolase NudC
  • EC number
  • Short names
    DeNADding enzyme NudC
  • Alternative names
    • NADH pyrophosphatase
      (EC:3.6.1.22
      ) . EC:3.6.1.22 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      nudC
    • ORF names
      MKS10_25975

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • K5-229
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella

Accessions

  • Primary accession
    A0AAE3RN80

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Structure

3D structure databases

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain125-248Nudix hydrolase
Motif159-180Nudix box

Sequence similarities

Belongs to the Nudix hydrolase family. NudC subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    257
  • Mass (Da)
    29,549
  • Last updated
    2024-05-29 v1
  • Checksum
    911EBF76574575BB
MDRIIEKLDRGWWVVSHEQKLWLPGGELPHGEAVNFDLVGQHALHIGEWQGESVWMVRQDRRHDMGSLRQVLDQDPGLFQLAGRGIQLAEFYRSHKFCGYCGHPMHASKSEWAMLCSHCRERYYPQIAPCIIVAIRRDDAILLAQHTRHRNGVHTVLAGFVEVGETLEQAVAREVMEESGIRVKNLRYVTSQPWPFPQSLMTAFMADYADGEIVVDKKELLTADWYRYDDLPLLPPPGTVARRLIEDTVAMCRAEFE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAKUZO010000028
EMBL· GenBank· DDBJ
MDK1967691.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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