Nudt19
entrez
110959
canonical
uniprot
P11930
canonical
ensembl
ENSMUSG00000034875
resolver
ensp
ENSMUSP00000047778
resolver
enst
ENSMUST00000040962
resolver
genesymbol
Nudt19
resolver
genesymbol_syn
D7Rp2e
resolver
uniprot
B2RS21
resolver
uniprot_entry
NUD19_MOUSE
resolver
uniprot_sec
B2RS21
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by chenodeoxycholic acid (CDCA) and its conjugated derivatives, taurochenodeoxycholic acid and glycochenodeoxycholic acid (PubMed:29378847). Inhibited by fluoride (PubMed:16185196). {ECO:0000269|PubMed:16185196, ECO:0000269|PubMed:29378847}.
uniprot
proteins
amino_acid_sequence
MSSSSSWRRAATVMLAAGWTHSSPAGFRLLLLQRAQNQRFLPGAHVFPGGVLDAADSSPDWVRLFAPRHTPPRFGLGPEPPRQPPFPGLSHGDADPAALPDDVALRICAIREAFEEAGVLLLRPRDAAPASQEPSQALSPPAGLAEWRSRVRSDPRCFLQLCAHLDCTPDIWALHDWGGWLTPYGRTIRRFDTTFFLCCLRDIPRVEPDVAEVVGYQWLSPSEATECFLSKEIWLAPPQFYEMRRLENFASLSALYRFCSDRPSEVPEKWLPIILLTSDGTIHLLPGDELYVKDSDFLEKNMSTDKKTEEIVKEGKVLNRVVIHSPYVYEIYMTLPSENKHVYPRNYIVNKRCTAHL
uniprot
proteins
ec_number
3.6.1.-
uniprot
proteins
ec_number
3.6.1.77
uniprot
proteins
function
FUNCTION: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (PubMed:16185196, PubMed:29378847). Mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters and at low substrate concentrations medium and long-chain fatty-acyl-CoA esters are the primary substrates (PubMed:16185196, PubMed:29378847). Highest activity seen with medium-chain acyl-CoA esters and higher rates of activity seen with the unsaturated acyl-CoA esters compared with the saturated esters (PubMed:16185196). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (PubMed:32432673). {ECO:0000269|PubMed:16185196, ECO:0000269|PubMed:29378847, ECO:0000269|PubMed:32432673}.
uniprot
proteins
mass_dalton
40320
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="R->M: 2-fold increase in Km for CoA. Reduced affinity for CoA."; /evidence="ECO:0000269|PubMed:29378847"; MUTAGEN 39; /note="R->A: No significant effect on Km for CoA."; /evidence="ECO:0000269|PubMed:29378847"; MUTAGEN 40; /note="F->A: 3- to 4-fold increase in Km for CoA. Reduced affinity for CoA."; /evidence="ECO:0000269|PubMed:29378847"; MUTAGEN 41; /note="L->A: 3- to 4-fold increase in Km for CoA. Reduced affinity for CoA."; /evidence="ECO:0000269|PubMed:29378847"; MUTAGEN 53; /note="D->A: No significant effect on Km for CoA."; /evidence="ECO:0000269|PubMed:29378847"; MUTAGEN 112; /note="E->A: Loss of fatty acyl-coenzyme A diphosphatase activity."; /evidence="ECO:0000269|PubMed:29378847"; MUTAGEN 115; /note="E->A: 3-fold increase in Km for CoA."; /evidence="ECO:0000269|PubMed:29378847"; MUTAGEN 116; /note="E->A: Loss of fatty acyl-coenzyme A diphosphatase activity."; /evidence="ECO:0000269|PubMed:29378847"; MUTAGEN 189; /note="R->A: 4-fold increase in Km for CoA. Reduced affinity for CoA."; /evidence="ECO:0000269|PubMed:29378847"; MUTAGEN 189; /note="R->M: No significant effect on Km for CoA."; /evidence="ECO:0000269|PubMed:29378847
uniprot
proteins
protein_family
Nudix hydrolase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16185196
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
29378847
uniprot
proteins
pubmed
32432673
uniprot
proteins
pubmed
3755524
uniprot
proteins
sequence_length
357
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16185196, ECO:0000269|PubMed:29378847}.
uniprot
proteins