P53164 · NPY1_YEAST

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 RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity).
Mediates the hydrolysis of some nucleoside diphosphate derivatives (PubMed:11361135).

Miscellaneous

Present with 846 molecules/cell in log phase SD medium.

Catalytic activity

Cofactor

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

Note: Binds 3 Mg2+ ions per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.17 mMNADH
0.5 mMNAD+
1.3 mMADP-ribose
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
2 μmol/min/mgwith NADH as substrate
0.85 μmol/min/mgwith NAD+ as substrate
0.8 μmol/min/mgwith ADP-ribose as substrate
kcat is 1.5 sec-1 for NADH. kcat is 0.6 sec-1 for NAD+. kcat is 0.6 sec-1 for ADP-ribose.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site179Zn2+ (UniProtKB | ChEBI)
Binding site182Zn2+ (UniProtKB | ChEBI)
Binding site197Zn2+ (UniProtKB | ChEBI)
Binding site206Zn2+ (UniProtKB | ChEBI)
Binding site256Mg2+ 1 (UniProtKB | ChEBI)
Binding site256-258substrate
Binding site272Mg2+ 2 (UniProtKB | ChEBI)
Binding site272Mg2+ 3 (UniProtKB | ChEBI)
Binding site272substrate
Binding site276Mg2+ 1 (UniProtKB | ChEBI)
Binding site276Mg2+ 3 (UniProtKB | ChEBI)
Binding site276substrate
Binding site322Mg2+ 1 (UniProtKB | ChEBI)
Binding site322Mg2+ 3 (UniProtKB | ChEBI)
Binding site322substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentperoxisome
Molecular Functionmetal ion binding
Molecular FunctionNAD+ diphosphatase activity
Molecular FunctionNADH pyrophosphatase activity
Molecular FunctionRNA NAD-cap (NMN-forming) hydrolase activity
Biological ProcessNAD catabolic process
Biological ProcessNAD-cap decapping
Biological ProcessNADH metabolic process
Biological ProcessNADP catabolic process
Biological ProcessRNA decapping

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NAD-capped RNA hydrolase NPY1
  • EC number
  • Short names
    DeNADding enzyme NPY1
  • Alternative names
    • NADH pyrophosphatase (EC:3.6.1.22
      ) . EC:3.6.1.22 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      NPY1
    • Ordered locus names
      YGL067W

Organism names

Accessions

  • Primary accession
    P53164
  • Secondary accessions
    • D6VU74
    • E9P928

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000569611-384NAD-capped RNA hydrolase NPY1

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain219-351Nudix hydrolase
Motif257-278Nudix box
Motif378-380Microbody targeting signal

Sequence similarities

Belongs to the Nudix hydrolase family. NudC subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    384
  • Mass (Da)
    43,516
  • Last updated
    1996-10-01 v1
  • Checksum
    96D6768CE2BC8F0B
MSTAVTFFGQHVLNRVSFLRCSKEFIKKSLNHDSTVFIPFIEGEALISPENGDLVQLSNSVKSYKNILSAIVPLYTTLLNTTRSRSDESGINVTFLGLLEGTDSAFNFEWSNISYKGTPYFGLDIRVTESTLFKKVDFEPIFSYPKVTRDHIFKQTNEDASLYSQGKMYLDWLAKYKFCPGCGSPLFPVEAGTKLQCSNENRNVYCNVRDARINNVCFPRTDPTVIIALTNSDYSKCCLARSKKRYGDFVLYSTIAGFMEPSETIEEACIREIWEETGISCKNIDIVRSQPWPYPCSLMIGCLGIVQFNSKNEVINLNHDDELLDAQWFDTTEIIQALDKYAGGYRVPFKNDINLPGSTTIAFQLINHVCENYKNLRKTSSSHL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict44in Ref. 3; AAT93207

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z72589
EMBL· GenBank· DDBJ
CAA96771.1
EMBL· GenBank· DDBJ
Genomic DNA
AY693188
EMBL· GenBank· DDBJ
AAT93207.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006941
EMBL· GenBank· DDBJ
DAA08035.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp