Q8GYB1 · NUD15_ARATH
- ProteinNudix hydrolase 15, mitochondrial
- GeneNUDT15
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids285 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
118.7 μM | CoA |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
1.4 μmol/min/mg | with CoA as substrate |
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | coenzyme A diphosphatase activity | |
Molecular Function | guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity | |
Molecular Function | metal ion binding | |
Biological Process | coenzyme A biosynthetic process | |
Biological Process | nucleoside phosphate metabolic process | |
Biological Process | succinyl-CoA metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNudix hydrolase 15, mitochondrial
- EC number
- Short namesAtNUDT15
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8GYB1
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
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.
PTM/Processing
Features
Showing features for transit peptide, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-23 | Mitochondrion | ||||
Sequence: MFLLYRRLPSFARTTTTTLLCKS | ||||||
Modified residue | 24 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000019958 | 24-285 | Nudix hydrolase 15, mitochondrial | |||
Sequence: MEPAITATSSSSFGGGSSRLAALAQQLRQYKPPPSSSFDDSEEMQTDQETAGKVVSQVGFQESIAPLSKDPDRFKPKRAAVLICLFEGDDGDLRVILTKRSSKLSTHSGEVSLPGGKAEEDDKDDGMTATREAEEEIGLDPSLVDVVTSLEPFLSKHLLRVIPVIGILRDKNKFNPIPNPGEVEAVFDAPLEMFLKDENRRSEEREWMGEKYLIHYFDYRTGDKDYMIWGLTAGILIRAASVTYERPPAFIEQCPKFKYPKM |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in roots, leaves, stems and inflorescences.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 51-72 | Disordered | ||||
Sequence: RQYKPPPSSSFDDSEEMQTDQE | ||||||
Domain | 99-255 | Nudix hydrolase | ||||
Sequence: PKRAAVLICLFEGDDGDLRVILTKRSSKLSTHSGEVSLPGGKAEEDDKDDGMTATREAEEEIGLDPSLVDVVTSLEPFLSKHLLRVIPVIGILRDKNKFNPIPNPGEVEAVFDAPLEMFLKDENRRSEEREWMGEKYLIHYFDYRTGDKDYMIWGLT | ||||||
Region | 129-152 | Disordered | ||||
Sequence: THSGEVSLPGGKAEEDDKDDGMTA | ||||||
Compositional bias | 137-152 | Basic and acidic residues | ||||
Sequence: PGGKAEEDDKDDGMTA | ||||||
Motif | 140-161 | Nudix box | ||||
Sequence: KAEEDDKDDGMTATREAEEEIG |
Sequence similarities
Belongs to the Nudix hydrolase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe 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.
- Name1
- Length285
- Mass (Da)31,898
- Last updated2005-07-05 v2
- ChecksumC790D52CA9DF2AB8
Q8GYB1-2
- Name2
- NoteMay be due to an intron retention.
- Differences from canonical
- 254-285: Missing
Q8GYB1-3
- Name3
- Differences from canonical
- 285-285: M → MVEKHTCMP
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |