NUD19_MOUSE
ID NUD19_MOUSE Reviewed; 357 AA.
AC P11930; B2RS21;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Acyl-coenzyme A diphosphatase NUDT19 {ECO:0000303|PubMed:29378847};
DE EC=3.6.1.-;
DE AltName: Full=Androgen-regulated protein RP2;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 19;
DE Short=Nudix motif 19;
DE AltName: Full=Renal CoA diphosphohydrolase {ECO:0000303|PubMed:29378847};
DE AltName: Full=Testosterone-regulated RP2 protein;
DE Short=RP2p;
GN Name=Nudt19; Synonyms=D7Rp2e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=DBA/LIHA; TISSUE=Kidney;
RX PubMed=3755524; DOI=10.1093/nar/14.13.5159;
RA King D., Sun Y.H., Lingrel J.B.;
RT "Amino acid sequence of the testosterone-regulated mouse kidney RP2 protein
RT deduced from its complementary DNA sequence.";
RL Nucleic Acids Res. 14:5159-5170(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=16185196; DOI=10.1042/bj20050893;
RA Ofman R., Speijer D., Leen R., Wanders R.J.A.;
RT "Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as
RT a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity.";
RL Biochem. J. 393:537-543(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-300, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, ACTIVITY REGULATION,
RP SUBUNIT, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, COFACTOR, COENZYME A BINDING SITES, MAGNESIUM BINDING SITES, AND
RP MUTAGENESIS OF ARG-34; ARG-39; PHE-40; LEU-41; ASP-53; GLU-112; GLU-115;
RP GLU-116 AND ARG-189.
RX PubMed=29378847; DOI=10.1074/jbc.ra117.001358;
RA Shumar S.A., Kerr E.W., Geldenhuys W.J., Montgomery G.E., Fagone P.,
RA Thirawatananond P., Saavedra H., Gabelli S.B., Leonardi R.;
RT "Nudt19 is a renal CoA diphosphohydrolase with biochemical and regulatory
RT properties that are distinct from the hepatic Nudt7 isoform.";
RL J. Biol. Chem. 293:4134-4148(2018).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32432673; DOI=10.1093/nar/gkaa402;
RA Sharma S., Grudzien-Nogalska E., Hamilton K., Jiao X., Yang J., Tong L.,
RA Kiledjian M.;
RT "Mammalian Nudix proteins cleave nucleotide metabolite caps on RNAs.";
RL Nucleic Acids Res. 48:6788-6798(2020).
CC -!- FUNCTION: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes
CC fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-
CC bisphosphate (PubMed:16185196, PubMed:29378847). Mediates the
CC hydrolysis of a wide range of CoA esters, including choloyl-CoA and
CC branched-chain fatty-acyl-CoA esters and at low substrate
CC concentrations medium and long-chain fatty-acyl-CoA esters are the
CC primary substrates (PubMed:16185196, PubMed:29378847). Highest activity
CC seen with medium-chain acyl-CoA esters and higher rates of activity
CC seen with the unsaturated acyl-CoA esters compared with the saturated
CC esters (PubMed:16185196). Exhibits decapping activity towards dpCoA-
CC capped RNAs in vitro (PubMed:32432673). {ECO:0000269|PubMed:16185196,
CC ECO:0000269|PubMed:29378847, ECO:0000269|PubMed:32432673}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-
CC phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58342, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:132023; Evidence={ECO:0000269|PubMed:16185196,
CC ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50045;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + H2O = (R)-4'-phosphopantetheine + adenosine 3',5'-
CC bisphosphate + 2 H(+); Xref=Rhea:RHEA:64988, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:61723; Evidence={ECO:0000269|PubMed:16185196,
CC ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64989;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC hexanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49980,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:62620, ChEBI:CHEBI:132012;
CC Evidence={ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49981;
CC Evidence={ECO:0000305|PubMed:29378847};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC S-octanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132013;
CC Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50017;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) +
CC S-butanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49976,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132011;
CC Evidence={ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49977;
CC Evidence={ECO:0000305|PubMed:29378847};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + propanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC propanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67464,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172362;
CC Evidence={ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67465;
CC Evidence={ECO:0000305|PubMed:29378847};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + malonyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC malonyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172363;
CC Evidence={ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67469;
CC Evidence={ECO:0000305|PubMed:29378847};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + succinyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC succinyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67472,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172364;
CC Evidence={ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67473;
CC Evidence={ECO:0000305|PubMed:29378847};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-
CC choloyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50036,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57373,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132020;
CC Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50037;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,8-dimethylnonanoyl-CoA + H2O = adenosine 3',5'-bisphosphate
CC + 2 H(+) + S-(4,8-dimethylnonanoyl)-4'-phosphopantetheine;
CC Xref=Rhea:RHEA:67524, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:77061, ChEBI:CHEBI:172385;
CC Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67525;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H2O = adenosine 3',5'-
CC bisphosphate + 2 H(+) + S-(9Z,12Z,15Z-octadecatrienoyl)-4'-
CC phosphopantetheine; Xref=Rhea:RHEA:67532, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, ChEBI:CHEBI:74034,
CC ChEBI:CHEBI:172386; Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67533;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = adenosine 3',5'-
CC bisphosphate + 2 H(+) + S-(9Z,12Z-octadecadienoyl)-4'-
CC phosphopantetheine; Xref=Rhea:RHEA:67536, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57383, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:172387; Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67537;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2
CC H(+) + S-(9Z-hexadecenoyl)-4'-phosphopantetheine;
CC Xref=Rhea:RHEA:67540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:61540, ChEBI:CHEBI:172388;
CC Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67541;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-tetradecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate +
CC 2 H(+) + S-(9Z-tetradecenoyl)-4'-phosphopantetheine;
CC Xref=Rhea:RHEA:67544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:65060, ChEBI:CHEBI:172389;
CC Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67545;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z)-octenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2
CC H(+) + S-(6Z-octenoyl)-4'-phosphopantetheine; Xref=Rhea:RHEA:67528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:172383, ChEBI:CHEBI:172384;
CC Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67529;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+)
CC + S-hexadecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50032,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132018;
CC Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50033;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = adenosine 3',5'-bisphosphate + 2
CC H(+) + tetradecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50028,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132017;
CC Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50029;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) +
CC S-dodecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50024,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132015;
CC Evidence={ECO:0000269|PubMed:16185196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50025;
CC Evidence={ECO:0000305|PubMed:16185196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = (R)-4'-
CC phosphopantetheine + a 5'-end phospho-adenosine-phospho-
CC ribonucleoside in mRNA + 2 H(+); Xref=Rhea:RHEA:67592, Rhea:RHEA-
CC COMP:15719, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:61723, ChEBI:CHEBI:144051,
CC ChEBI:CHEBI:172371; Evidence={ECO:0000305|PubMed:32432673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67593;
CC Evidence={ECO:0000305|PubMed:32432673};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16185196, ECO:0000269|PubMed:29378847};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16185196};
CC -!- ACTIVITY REGULATION: Inhibited by chenodeoxycholic acid (CDCA) and its
CC conjugated derivatives, taurochenodeoxycholic acid and
CC glycochenodeoxycholic acid (PubMed:29378847). Inhibited by fluoride
CC (PubMed:16185196). {ECO:0000269|PubMed:16185196,
CC ECO:0000269|PubMed:29378847}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for CoA {ECO:0000269|PubMed:16185196};
CC KM=0.58 mM for oxidized CoA {ECO:0000269|PubMed:16185196};
CC KM=0.08 mM for lauroyl-CoA {ECO:0000269|PubMed:16185196};
CC KM=0.01 mM for palmitoyl-CoA {ECO:0000269|PubMed:16185196};
CC KM=0.1 mM for choloyl-CoA {ECO:0000269|PubMed:16185196};
CC KM=0.1 mM for pristanoyl-CoA {ECO:0000269|PubMed:16185196};
CC KM=300 uM for CoA {ECO:0000269|PubMed:29378847};
CC Vmax=0.56 umol/min/mg enzyme with CoA as substrate
CC {ECO:0000269|PubMed:16185196};
CC Vmax=0.012 umol/min/mg enzyme with oxidized CoA as substrate
CC {ECO:0000269|PubMed:16185196};
CC Vmax=0.2 umol/min/mg enzyme with lauroyl-CoA as substrate
CC {ECO:0000269|PubMed:16185196};
CC Vmax=0.013 umol/min/mg enzyme with palmitoyl-CoA as substrate
CC {ECO:0000269|PubMed:16185196};
CC Vmax=0.17 umol/min/mg enzyme with choloyl-CoA as substrate
CC {ECO:0000269|PubMed:16185196};
CC Vmax=0.009 umol/min/mg enzyme with pristanoyl-CoA as substrate
CC {ECO:0000269|PubMed:16185196};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:16185196};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:29378847}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16185196,
CC ECO:0000269|PubMed:29378847}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the kidneys, with lower levels
CC in skeletal muscle and brain (at protein level).
CC {ECO:0000269|PubMed:29378847}.
CC -!- INDUCTION: By testosterone. {ECO:0000269|PubMed:3755524}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit a significant 20% increase in total
CC CoA levels in kidney. {ECO:0000269|PubMed:29378847}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; X04097; CAA27722.1; -; mRNA.
DR EMBL; BC138674; AAI38675.1; -; mRNA.
DR EMBL; BC138675; AAI38676.1; -; mRNA.
DR CCDS; CCDS21152.1; -.
DR PIR; A23641; A23641.
DR RefSeq; NP_149071.2; NM_033080.2.
DR AlphaFoldDB; P11930; -.
DR SMR; P11930; -.
DR BioGRID; 226054; 1.
DR IntAct; P11930; 2.
DR MINT; P11930; -.
DR STRING; 10090.ENSMUSP00000047778; -.
DR iPTMnet; P11930; -.
DR PhosphoSitePlus; P11930; -.
DR EPD; P11930; -.
DR jPOST; P11930; -.
DR MaxQB; P11930; -.
DR PaxDb; P11930; -.
DR PeptideAtlas; P11930; -.
DR PRIDE; P11930; -.
DR ProteomicsDB; 293779; -.
DR Antibodypedia; 44300; 99 antibodies from 19 providers.
DR Ensembl; ENSMUST00000040962; ENSMUSP00000047778; ENSMUSG00000034875.
DR GeneID; 110959; -.
DR KEGG; mmu:110959; -.
DR UCSC; uc009gka.1; mouse.
DR CTD; 390916; -.
DR MGI; MGI:94203; Nudt19.
DR VEuPathDB; HostDB:ENSMUSG00000034875; -.
DR eggNOG; KOG3904; Eukaryota.
DR GeneTree; ENSGT00420000029858; -.
DR HOGENOM; CLU_059078_1_0_1; -.
DR InParanoid; P11930; -.
DR OMA; SPHQGFM; -.
DR OrthoDB; 1417901at2759; -.
DR PhylomeDB; P11930; -.
DR TreeFam; TF313185; -.
DR Reactome; R-MMU-390918; Peroxisomal lipid metabolism.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 110959; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Nudt19; mouse.
DR PRO; PR:P11930; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P11930; protein.
DR Bgee; ENSMUSG00000034875; Expressed in right kidney and 260 other tissues.
DR Genevisible; P11930; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0106399; F:acyl-coenzyme A diphosphatase activity; IEA:RHEA.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0044580; P:butyryl-CoA catabolic process; IDA:UniProtKB.
DR GO; GO:0015938; P:coenzyme A catabolic process; IDA:UniProtKB.
DR GO; GO:2001294; P:malonyl-CoA catabolic process; IDA:UniProtKB.
DR GO; GO:0036114; P:medium-chain fatty-acyl-CoA catabolic process; IDA:UniProtKB.
DR GO; GO:1902858; P:propionyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:1901289; P:succinyl-CoA catabolic process; IDA:UniProtKB.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR039121; NUDT19.
DR PANTHER; PTHR12318; PTHR12318; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Peroxisome;
KW Reference proteome.
FT CHAIN 1..357
FT /note="Acyl-coenzyme A diphosphatase NUDT19"
FT /id="PRO_0000057119"
FT DOMAIN 10..242
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 72..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..118
FT /note="Nudix box"
FT MOTIF 355..357
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 73..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:29378847"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:29378847"
FT SITE 34
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000269|PubMed:29378847"
FT SITE 40
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000269|PubMed:29378847"
FT SITE 41
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000269|PubMed:29378847"
FT SITE 189
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000269|PubMed:29378847"
FT MOD_RES 300
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MUTAGEN 34
FT /note="R->M: 2-fold increase in Km for CoA. Reduced
FT affinity for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 39
FT /note="R->A: No significant effect on Km for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 40
FT /note="F->A: 3- to 4-fold increase in Km for CoA. Reduced
FT affinity for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 41
FT /note="L->A: 3- to 4-fold increase in Km for CoA. Reduced
FT affinity for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 53
FT /note="D->A: No significant effect on Km for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 112
FT /note="E->A: Loss of fatty acyl-coenzyme A diphosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 115
FT /note="E->A: 3-fold increase in Km for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 116
FT /note="E->A: Loss of fatty acyl-coenzyme A diphosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 189
FT /note="R->A: 4-fold increase in Km for CoA. Reduced
FT affinity for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 189
FT /note="R->M: No significant effect on Km for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT CONFLICT 203
FT /note="I -> T (in Ref. 1; CAA27722)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="C -> Y (in Ref. 1; CAA27722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 40320 MW; 6ED30EC4BF2955FE CRC64;
MSSSSSWRRA ATVMLAAGWT HSSPAGFRLL LLQRAQNQRF LPGAHVFPGG VLDAADSSPD
WVRLFAPRHT PPRFGLGPEP PRQPPFPGLS HGDADPAALP DDVALRICAI REAFEEAGVL
LLRPRDAAPA SQEPSQALSP PAGLAEWRSR VRSDPRCFLQ LCAHLDCTPD IWALHDWGGW
LTPYGRTIRR FDTTFFLCCL RDIPRVEPDV AEVVGYQWLS PSEATECFLS KEIWLAPPQF
YEMRRLENFA SLSALYRFCS DRPSEVPEKW LPIILLTSDG TIHLLPGDEL YVKDSDFLEK
NMSTDKKTEE IVKEGKVLNR VVIHSPYVYE IYMTLPSENK HVYPRNYIVN KRCTAHL
