Q8WV74 · NUDT8_HUMAN
- ProteinMitochondrial coenzyme A diphosphatase NUDT8
- GeneNUDT8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids236 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acyl-CoA diphosphatase that mediates the hydrolysis of a wide range of CoA and CoA esters yielding 3',5'-ADP and the corresponding 4'-phosphopantetheine derivative as products (By similarity).
Hydrolyzes short- and medium-chain acyl-CoAs, exhibiting the highest activity toward free CoA, hexanoyl-CoA, and octanoyl-CoA and the lowest activity against acetyl-CoA (By similarity).
Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
Hydrolyzes short- and medium-chain acyl-CoAs, exhibiting the highest activity toward free CoA, hexanoyl-CoA, and octanoyl-CoA and the lowest activity against acetyl-CoA (By similarity).
Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
Catalytic activity
- an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-phosphopantetheine + 2 H+This reaction proceeds in the forward direction.
- acetyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H+ + S-acetyl-4'-phosphopantetheineThis reaction proceeds in the forward direction.
- butanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H+ + S-butanoyl-4'-phosphopantetheineThis reaction proceeds in the forward direction.
- H2O + hexanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H+ + hexanoyl-4'-phosphopantetheineThis reaction proceeds in the forward direction.
- H2O + octanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H+ + S-octanoyl-4'-phosphopantetheineThis reaction proceeds in the forward direction.
- H2O + propanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H+ + propanoyl-4'-phosphopantetheineThis reaction proceeds in the forward direction.
- H2O + malonyl-CoA = adenosine 3',5'-bisphosphate + 2 H+ + malonyl-4'-phosphopantetheineThis reaction proceeds in the forward direction.
- H2O + succinyl-CoA = adenosine 3',5'-bisphosphate + 2 H+ + succinyl-4'-phosphopantetheineThis reaction proceeds in the forward direction.
- a 5'-end CoA-ribonucleoside in mRNA + H2O = (R)-4'-phosphopantetheine + a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + 2 H+This reaction proceeds in the forward direction.
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | coenzyme A diphosphatase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | manganese ion binding | |
Biological Process | acetyl-CoA catabolic process | |
Biological Process | butyryl-CoA catabolic process | |
Biological Process | coenzyme A catabolic process | |
Biological Process | malonyl-CoA catabolic process | |
Biological Process | medium-chain fatty-acyl-CoA catabolic process | |
Biological Process | propionyl-CoA catabolic process | |
Biological Process | succinyl-CoA catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitochondrial coenzyme A diphosphatase NUDT8
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8WV74
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 299 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000019948 | 1-236 | Mitochondrial coenzyme A diphosphatase NUDT8 | |||
Sequence: MLPDCLSAEGELRCRRLLAGATARLRARPASAAVLVPLCSVRGVPALLYTLRSSRLTGRHKGDVSFPGGKCDPADQDVVHTALRETREELGLAVPEEHVWGLLRPVYDPQKATVVPVLAGVGPLDPQSLRPNSEEVDEVFALPLAHLLQTQNQGYTHFCRGGHFRYTLPVFLHGPHRVWGLTAVITEFALQLLAPGTYQPRLAGLTCSGAEGLARPKQPLASPCQASSTPGLNKGL | ||||||
Modified residue | 70 | N6-succinyllysine | ||||
Sequence: K |
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-172 | Nudix hydrolase | ||||
Sequence: LRARPASAAVLVPLCSVRGVPALLYTLRSSRLTGRHKGDVSFPGGKCDPADQDVVHTALRETREELGLAVPEEHVWGLLRPVYDPQKATVVPVLAGVGPLDPQSLRPNSEEVDEVFALPLAHLLQTQNQGYTHFCRGGHFRYTLPVFL | ||||||
Motif | 70-91 | Nudix box | ||||
Sequence: KCDPADQDVVHTALRETREELG |
Sequence similarities
Belongs to the Nudix hydrolase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8WV74-1
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
- Length236
- Mass (Da)25,370
- Last updated2005-07-05 v2
- Checksum7DDD2A56010B4D9F
Q8WV74-2
- Name2
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK123561 EMBL· GenBank· DDBJ | BAC85646.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018644 EMBL· GenBank· DDBJ | AAH18644.1 EMBL· GenBank· DDBJ | mRNA |