NUD19_MUSSA
ID NUD19_MUSSA Reviewed; 356 AA.
AC Q7M0H4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Acyl-coenzyme A diphosphatase NUDT19;
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=Testosterone-regulated RP2 protein;
DE Short=RP2p;
GN Name=Nudt19;
OS Mus saxicola (Brown spiny mouse) (Rock-loving mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Pyromys.
OX NCBI_TaxID=10094;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1766361; DOI=10.1093/oxfordjournals.molbev.a040675;
RA Chaudhuri A., Barbour K.W., Berger F.G.;
RT "Evolution of messenger RNA structure and regulation in the genus Mus: the
RT androgen-inducible RP2 mRNAs.";
RL Mol. Biol. Evol. 8:641-653(1991).
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 (By similarity). Mediates the hydrolysis of a wide range
CC of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA
CC esters and at low substrate concentrations medium and long-chain fatty-
CC acyl-CoA esters are the primary substrates (By similarity). Highest
CC activity seen with medium-chain acyl-CoA esters and higher rates of
CC activity seen with the unsaturated acyl-CoA esters compared with the
CC saturated esters (By similarity). Exhibits decapping activity towards
CC dpCoA-capped RNAs in vitro (By similarity).
CC {ECO:0000250|UniProtKB:P11930}.
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50045;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64989;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49981;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50017;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49977;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67465;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67469;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67473;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50037;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67525;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67533;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67537;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67541;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67545;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67529;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50033;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50029;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50025;
CC Evidence={ECO:0000250|UniProtKB:P11930};
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:0000250|UniProtKB:P11930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67593;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P11930};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P11930}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P11930}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; B39798; B39798.
DR AlphaFoldDB; Q7M0H4; -.
DR SMR; Q7M0H4; -.
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; ISS:UniProtKB.
DR GO; GO:0044580; P:butyryl-CoA catabolic process; ISS:UniProtKB.
DR GO; GO:0015938; P:coenzyme A catabolic process; ISS:UniProtKB.
DR GO; GO:2001294; P:malonyl-CoA catabolic process; ISS:UniProtKB.
DR GO; GO:0036114; P:medium-chain fatty-acyl-CoA catabolic process; ISS:UniProtKB.
DR GO; GO:1902858; P:propionyl-CoA metabolic process; ISS:UniProtKB.
DR GO; GO:1901289; P:succinyl-CoA catabolic process; ISS: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 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Peroxisome.
FT CHAIN 1..356
FT /note="Acyl-coenzyme A diphosphatase NUDT19"
FT /id="PRO_0000324573"
FT DOMAIN 10..241
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 72..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..118
FT /note="Nudix box"
FT MOTIF 354..356
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:0000250|UniProtKB:P11930"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 34
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 40
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 41
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 188
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT MOD_RES 299
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11930"
SQ SEQUENCE 356 AA; 40221 MW; 039CD9CE6BA1F729 CRC64;
MSGQSSWRRA ATVMLAAGWT HSSPAGFRLL LLQRAQNQRF LPGAHVFPGG VLDAADSSPD
WVRLFAPRHT PPRFGLGPEP PRQPPFPGLS HGDADPAALP DDVALRICAI RETFEEAGVL
LLRPRDAPAS QEPSQALSPP AGLAEWRSRV RSDPRCFLQL CAHLDCTPDI WALHDWGGWL
TPYGRSLRRF DTTFLLCCLR DTPRVEPDLA EVVGYQWLSP SEATECFLSK EIWLAPPQFY
EMRRLENFAS LSALYRFCSD RPLEVAQKWL PIILVTSDGS VHLLPGDELY VKDSDFLEKN
MSTDKKTEEI MKEGKVLNRI VIRSPYVYEI YVTLPSENKH VFPRNYIVNK SRTARL
