A0A2K9PGD6 · A0A2K9PGD6_9ENTR

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.

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 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
    • ORF names
      WM46_21135

Organism names

  • Taxonomic identifier
  • Strain
    • CFNIH2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Citrobacter > Citrobacter freundii complex

Accessions

  • Primary accession
    A0A2K9PGD6

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

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)
    29,597
  • Last updated
    2018-04-25 v1
  • Checksum
    044941C89E609094
MDRIIEKLDHGWWIVSHEQKLWLPHGELPHGDAANFDLVGQPALQIGEWEGEPVWLVLQHRRHEMGSVRQVLDQDAGLFQLAGRGVQLAEFYRSHKFCGYCGHPMQPSKTEWAMLCTHCRERYYPQIAPCIIVAIRREDSILLAQHVRHRNGVHTVLAGFVEVGETLEQAVAREVMEESGIKIKNLRYITSQPWPFPMSLMTAFMAEYDSGEIVIDPKELLEANWYRYDDLPLLPPPGTVARRLIEDTVAMCRAEYE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP025757
EMBL· GenBank· DDBJ
AUO67033.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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