NUD19_CHICK
ID NUD19_CHICK Reviewed; 378 AA.
AC Q5ZL13;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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; ORFNames=RCJMB04_8e7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719921; CAG31580.1; -; mRNA.
DR RefSeq; NP_001026629.1; NM_001031458.1.
DR AlphaFoldDB; Q5ZL13; -.
DR STRING; 9031.ENSGALP00000038637; -.
DR Ensembl; ENSGALT00000048378; ENSGALP00000050272; ENSGALG00000029498.
DR GeneID; 427548; -.
DR KEGG; gga:427548; -.
DR CTD; 390916; -.
DR VEuPathDB; HostDB:geneid_427548; -.
DR eggNOG; KOG3904; Eukaryota.
DR GeneTree; ENSGT00420000029858; -.
DR InParanoid; Q5ZL13; -.
DR OMA; SPHQGFM; -.
DR OrthoDB; 1417901at2759; -.
DR PhylomeDB; Q5ZL13; -.
DR PRO; PR:Q5ZL13; -.
DR Proteomes; UP000000539; Chromosome 11.
DR Bgee; ENSGALG00000029498; Expressed in spermatid and 13 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..378
FT /note="Acyl-coenzyme A diphosphatase NUDT19"
FT /id="PRO_0000324575"
FT DOMAIN 7..258
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 105..126
FT /note="Nudix box"
FT MOTIF 376..378
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 41
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 47
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
FT SITE 205
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000250|UniProtKB:P11930"
SQ SEQUENCE 378 AA; 42122 MW; AFCE6866961407D4 CRC64;
MNPRLRHWRE AASVLLAAGA PGRRSPSPLG PCDYELLFLQ RSSRSGFMPS AHVFPGGLVE
AADFSAEWLR LLPAAPRCGL GAVRPPPPGG SRAPLFATDR QPLGSPLPGE VAFRICAIRE
TFEEAGILLL APGGRPREGS GPAPSLPAEQ LLPAAELGEW RRRVQEDPAC FLQLCQRLGR
VPDIWALQEW SNWLTPVGRA GRGGRRYDTA FYLCCLETRP PHTSQDNQEI AAFLWSSPPE
AIERFKSQEI WLAPPQFYEL CRLCNFSSLN DLHKFSSDRA LEGCERWLPV TLTAADGFIQ
LLPGDELYPE DPDYTGEKKI TMSTDKMVED LMKEGSVFHR IVIKNTHSLA VYVNIQAKYK
HMNPLMINTD SSNYNSRL
