Q8GYB1 · NUD15_ARATH

Function

function

Coenzyme A diphosphatase which mediates the cleavage of oxidized CoA. Can use malonyl-CoA, hexanoyl-CoA, lauroyl-CoA, myristoyl-CoA and palmitoyl-CoA as substrates, but not isobutyryl-CoA or propionyl-CoA.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
118.7 μMCoA
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
1.4 μmol/min/mgwith CoA as substrate

Features

Showing features for binding site.

128520406080100120140160180200220240260280
TypeIDPosition(s)Description
Binding site155Mg2+ (UniProtKB | ChEBI)
Binding site159Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Molecular Functioncoenzyme A diphosphatase activity
Molecular Functionguanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
Molecular Functionmetal ion binding
Biological Processcoenzyme A biosynthetic process
Biological Processnucleoside phosphate metabolic process
Biological Processsuccinyl-CoA metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nudix hydrolase 15, mitochondrial
  • EC number
  • Short names
    AtNUDT15
  • Alternative names
    • Coenzyme A diphosphatase NUDT15

Gene names

    • Name
      NUDT15
    • Synonyms
      NUDX15
    • ORF names
      F1K23.16, F1K23.5
    • Ordered locus names
      At1g28960

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q8GYB1
  • Secondary accessions
    • Q0WKX6
    • Q3E701
    • Q3E702
    • Q67YK3
    • Q9SHQ7

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

No visible phenotype under normal growth conditions.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 15 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, modified residue, chain.

TypeIDPosition(s)Description
Transit peptide1-23Mitochondrion
Modified residue24N-acetylmethionine
ChainPRO_000001995824-285Nudix hydrolase 15, mitochondrial

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in roots, leaves, stems and inflorescences.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias, motif.

TypeIDPosition(s)Description
Region51-72Disordered
Domain99-255Nudix hydrolase
Region129-152Disordered
Compositional bias137-152Basic and acidic residues
Motif140-161Nudix box

Sequence similarities

Belongs to the Nudix hydrolase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 3 isoforms produced by Alternative splicing.

Q8GYB1-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    285
  • Mass (Da)
    31,898
  • Last updated
    2005-07-05 v2
  • Checksum
    C790D52CA9DF2AB8
MFLLYRRLPSFARTTTTTLLCKSMEPAITATSSSSFGGGSSRLAALAQQLRQYKPPPSSSFDDSEEMQTDQETAGKVVSQVGFQESIAPLSKDPDRFKPKRAAVLICLFEGDDGDLRVILTKRSSKLSTHSGEVSLPGGKAEEDDKDDGMTATREAEEEIGLDPSLVDVVTSLEPFLSKHLLRVIPVIGILRDKNKFNPIPNPGEVEAVFDAPLEMFLKDENRRSEEREWMGEKYLIHYFDYRTGDKDYMIWGLTAGILIRAASVTYERPPAFIEQCPKFKYPKM

Q8GYB1-2

  • Name
    2
  • Note
    May be due to an intron retention.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q8GYB1-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence AAF24540.2 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias137-152Basic and acidic residues
Alternative sequenceVSP_015093254-285in isoform 2
Sequence conflict264in Ref. 3; BAC42400
Alternative sequenceVSP_037560285in isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC007508
EMBL· GenBank· DDBJ
AAF24540.2
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002684
EMBL· GenBank· DDBJ
AEE31022.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE31024.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE31026.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM58454.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM58455.1
EMBL· GenBank· DDBJ
Genomic DNA
AK117752
EMBL· GenBank· DDBJ
BAC42400.1
EMBL· GenBank· DDBJ
mRNA
AK175332
EMBL· GenBank· DDBJ
BAD43095.1
EMBL· GenBank· DDBJ
mRNA
AK176465
EMBL· GenBank· DDBJ
BAD44228.1
EMBL· GenBank· DDBJ
mRNA
AK221329
EMBL· GenBank· DDBJ
BAD94135.1
EMBL· GenBank· DDBJ
mRNA
AK228486
EMBL· GenBank· DDBJ
BAF00412.1
EMBL· GenBank· DDBJ
mRNA
AK230433
EMBL· GenBank· DDBJ
BAF02231.1
EMBL· GenBank· DDBJ
mRNA
AK317052
EMBL· GenBank· DDBJ
BAH19745.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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