NDX3_CAEEL
ID NDX3_CAEEL Reviewed; 240 AA.
AC Q23236;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Nudix hydrolase 3;
DE EC=3.6.1.-;
GN Name=ndx-3; ORFNames=Y38A8.1;
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 [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: Probably mediates the hydrolysis of some nucleoside
CC diphosphate derivatives. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; FO081756; CCD73693.1; -; Genomic_DNA.
DR PIR; T26648; T26648.
DR RefSeq; NP_494912.2; NM_062511.3.
DR AlphaFoldDB; Q23236; -.
DR SMR; Q23236; -.
DR STRING; 6239.Y38A8.1; -.
DR EPD; Q23236; -.
DR PaxDb; Q23236; -.
DR PeptideAtlas; Q23236; -.
DR PRIDE; Q23236; -.
DR EnsemblMetazoa; Y38A8.1.1; Y38A8.1.1; WBGene00003580.
DR UCSC; Y38A8.1; c. elegans.
DR WormBase; Y38A8.1; CE45628; WBGene00003580; ndx-3.
DR eggNOG; KOG3069; Eukaryota.
DR HOGENOM; CLU_040940_4_1_1; -.
DR InParanoid; Q23236; -.
DR OMA; YYIWGAT; -.
DR OrthoDB; 1253012at2759; -.
DR PhylomeDB; Q23236; -.
DR PRO; PR:Q23236; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003580; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0015938; P:coenzyme A catabolic process; IBA:GO_Central.
DR GO; GO:0009132; P:nucleoside diphosphate metabolic process; IEA:InterPro.
DR CDD; cd03426; CoAse; 1.
DR InterPro; IPR045121; CoAse.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR000059; NUDIX_hydrolase_NudL_CS.
DR PANTHER; PTHR12992; PTHR12992; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
DR PROSITE; PS01293; NUDIX_COA; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..240
FT /note="Nudix hydrolase 3"
FT /id="PRO_0000057144"
FT DOMAIN 50..190
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 89..110
FT /note="Nudix box"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 240 AA; 27098 MW; 517FCC2073E630A8 CRC64;
MRYGLSAQRS LINVCSRRFF GKDAKEQFLK NLSSIPASKH PRLVSDSDAN SAMSVLIPLV
TVDGRDSVLL TKRSIHLRSH RGEVCFPGGR MDPGETTTET ALRETFEEIG VNAESVEIWG
HLKSVIRRQA DFNVTPIVGY ISDERVLENL VVNSDEVQAV FTIPIDELIK KAGLTKFQSK
RMKYTLPSFD STEFKVHHNA PNEYLHSTQR VWGLSGVMLH QALTLLNPDV YKHDLIVKFF
