NUD19_XENLA
ID NUD19_XENLA Reviewed; 380 AA.
AC Q5PQ50;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Acyl-coenzyme A diphosphatase NUDT19;
DE EC=3.6.1.-;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 19;
DE Short=Nudix motif 19;
GN Name=nudt19;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC087364; AAH87364.1; -; mRNA.
DR RefSeq; NP_001088716.1; NM_001095247.1.
DR AlphaFoldDB; Q5PQ50; -.
DR DNASU; 495980; -.
DR GeneID; 495980; -.
DR KEGG; xla:495980; -.
DR CTD; 495980; -.
DR Xenbase; XB-GENE-5839228; nudt19.L.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 495980; Expressed in muscle tissue and 20 other tissues.
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;
KW Reference proteome.
FT CHAIN 1..380
FT /note="Acyl-coenzyme A diphosphatase NUDT19"
FT /id="PRO_0000324576"
FT DOMAIN 8..264
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 115..136
FT /note="Nudix box"
FT MOTIF 378..380
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 51
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 57
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 212
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
SQ SEQUENCE 380 AA; 43762 MW; 0E4192B35E0F8D3E CRC64;
MNNTLKYWKE AATLIVAART SHGHFPYIQP QVQFPNQQNN TSDYEVLLLK RSQKSGFMPN
AFVFPGGNIE SSDFSSDWIK VFSRYEQKPN FGLGLVKQLD NRSPMFTADS SKFGSLIPGE
VATRICAIRE TFEESGILLV VPENFNSEDN QHLVEVTDQD KEKLSKWREE VQRNPSQFIQ
MCKEMRCMPN IWALKEWSNW LTPVISQGVK SRRFDTAFFI CCLNAKPAVS DDNKEVTSFK
WWTPTEALED YKSHKIWIPP PQFYELSRLC HFAPINELHK FIVNRSLEGC ERWMPVIAQC
EDGIVHTLPG DDLYPEDPDL TGEKQTVVCS NETIENLIQK GGRFHRLVLI DGKPTLLVNI
KPKYKHINPL TIESESKNKL
