Q6LLW5 · NUDC_PHOPR

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

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 site74substrate
Binding site103Zn2+ (UniProtKB | ChEBI)
Binding site106Zn2+ (UniProtKB | ChEBI)
Binding site121Zn2+ (UniProtKB | ChEBI)
Binding site124Zn2+ (UniProtKB | ChEBI)
Binding site129substrate
Binding site163a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site179a divalent metal cation 2 (UniProtKB | ChEBI)
Binding site179a divalent metal cation 3 (UniProtKB | ChEBI)
Binding site183a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site183a divalent metal cation 3 (UniProtKB | ChEBI)
Binding site197-204substrate
Binding site224a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site224a divalent metal cation 3 (UniProtKB | ChEBI)
Binding site246substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular FunctionNAD+ diphosphatase activity
Molecular FunctionNADH pyrophosphatase activity
Molecular FunctionRNA NAD-cap (NMN-forming) hydrolase 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
    • Ordered locus names
      PBPRA3429

Organism names

Accessions

  • Primary accession
    Q6LLW5

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000719601-266NAD-capped RNA hydrolase NudC

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, motif.

Type
IDPosition(s)Description
Domain130-253Nudix hydrolase
Motif164-185Nudix box

Sequence similarities

Belongs to the Nudix hydrolase family. NudC subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    266
  • Mass (Da)
    29,872
  • Last updated
    2004-07-05 v1
  • MD5 Checksum
    50DFAD514BB7810EC0A42CBE378A0CB7
MDVILMLNKRELAYWCVVNDRKLYLLDNAIPLLEKSELTFNTDSARVIGEYLDHPVYWLEANNCLHSDDFYTQRELLGIDQALFDLAGRATQLSHMLHTQSFCSVCGGAAVLADDQFAMVCQQCSNAQYPRVSPCIIVAVRKEDQILLAQHPRHKTGIYTVIAGFVEAGETLEQCVAREVEEETGIQVKNIRYFSSQPWAFPSNIMMAFLADYESGEINPDYEELSDAIWAKAAELPAIAPKGTIARVLIDETLALIKATKHVQNL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CR378674
EMBL· GenBank· DDBJ
CAG21713.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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