NDX8_CAEEL
ID NDX8_CAEEL Reviewed; 234 AA.
AC Q9NA25;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Peroxisomal coenzyme A diphosphatase ndx-8;
DE EC=3.6.1.-;
DE AltName: Full=Nudix hydrolase 8;
GN Name=ndx-8; ORFNames=Y87G2A.14;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 232-SER--ILE-234.
RX PubMed=11943069; DOI=10.1186/1471-2091-3-5;
RA AbdelRaheim S.R., McLennan A.G.;
RT "The Caenorhabditis elegans Y87G2A.14 Nudix hydrolase is a peroxisomal
RT coenzyme A diphosphatase.";
RL BMC Biochem. 3:5-5(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Coenzyme A diphosphatase which mediates the cleavage of CoA
CC into 3',5'-ADP and 4'-phosphopantetheine.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=220 uM for CoA {ECO:0000269|PubMed:11943069};
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:11943069};
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AL110500; CAB54476.1; -; Genomic_DNA.
DR PIR; T27454; T27454.
DR RefSeq; NP_493372.1; NM_060971.1.
DR AlphaFoldDB; Q9NA25; -.
DR SMR; Q9NA25; -.
DR BioGRID; 55353; 2.
DR DIP; DIP-24589N; -.
DR IntAct; Q9NA25; 1.
DR STRING; 6239.Y87G2A.14; -.
DR EPD; Q9NA25; -.
DR PaxDb; Q9NA25; -.
DR PeptideAtlas; Q9NA25; -.
DR EnsemblMetazoa; Y87G2A.14.1; Y87G2A.14.1; WBGene00003585.
DR GeneID; 190780; -.
DR KEGG; cel:CELE_Y87G2A.14; -.
DR UCSC; Y87G2A.14; c. elegans.
DR CTD; 190780; -.
DR WormBase; Y87G2A.14; CE23122; WBGene00003585; ndx-8.
DR eggNOG; KOG3069; Eukaryota.
DR GeneTree; ENSGT00940000162775; -.
DR HOGENOM; CLU_040940_6_0_1; -.
DR InParanoid; Q9NA25; -.
DR OMA; CPNPAEV; -.
DR OrthoDB; 1253012at2759; -.
DR PhylomeDB; Q9NA25; -.
DR Reactome; R-CEL-9033241; Peroxisomal protein import.
DR PRO; PR:Q9NA25; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003585; Expressed in larva and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IDA:WormBase.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:WormBase.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; IDA:WormBase.
DR GO; GO:0047994; F:hydroxymethylglutaryl-CoA hydrolase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004778; F:succinyl-CoA hydrolase activity; IDA:WormBase.
DR GO; GO:0015938; P:coenzyme A catabolic process; IDA:WormBase.
DR CDD; cd03426; CoAse; 1.
DR InterPro; IPR045121; CoAse.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR12992; PTHR12992; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Membrane; Metal-binding; Peroxisome;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..234
FT /note="Peroxisomal coenzyme A diphosphatase ndx-8"
FT /id="PRO_0000057138"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 27..162
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 66..90
FT /note="Nudix box"
FT MOTIF 232..234
FT /note="Microbody targeting signal"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 232..234
FT /note="Missing: Abolishes localization to peroxisomes."
FT /evidence="ECO:0000269|PubMed:11943069"
SQ SEQUENCE 234 AA; 26598 MW; 4920BB16F46DB81A CRC64;
MKCVVSRADD LKRMLDLSDV PTKSQGEQDA GVLILLHDDG SEKLKVLLCV RSRQLRRHPG
EVCFPGGMMD DEDGQNVRRT AIREAYEEVG VNENDDYLVL GNLPAFRARF GVLIHPTVAL
LRRPPTFVLS IGEVESIFWI PLSQFLEDTH HSTFLIDEFY MVHVFQFDEY PTTYGVTALM
CIVVAIGLLG KLPNFNLMGN LTISDMLDKH LDSIEIIRHV YEFASRKFEP KSKI
