ID   NUDL_SALPK              Reviewed;         192 AA.
AC   B5BHD1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Uncharacterized Nudix hydrolase NudL {ECO:0000255|HAMAP-Rule:MF_01592};
DE            EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01592};
GN   Name=nudL {ECO:0000255|HAMAP-Rule:MF_01592}; OrderedLocusNames=SSPA0978;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(2009).
CC   -!- FUNCTION: Probably mediates the hydrolysis of some nucleoside
CC       diphosphate derivatives. {ECO:0000255|HAMAP-Rule:MF_01592}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01592};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01592};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01592}.
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DR   EMBL; FM200053; CAR59129.1; -; Genomic_DNA.
DR   RefSeq; WP_000381531.1; NC_011147.1.
DR   AlphaFoldDB; B5BHD1; -.
DR   SMR; B5BHD1; -.
DR   KEGG; sek:SSPA0978; -.
DR   HOGENOM; CLU_040940_5_2_6; -.
DR   OMA; YYIWGAT; -.
DR   Proteomes; UP000001869; Chromosome.
DR   GO; GO:0010945; F:CoA pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009132; P:nucleoside diphosphate metabolic process; IEA:InterPro.
DR   CDD; cd03426; CoAse; 1.
DR   HAMAP; MF_01592; Nudix_NudL; 1.
DR   InterPro; IPR045121; CoAse.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR000059; NUDIX_hydrolase_NudL_CS.
DR   InterPro; IPR023735; Nudix_NudL.
DR   PANTHER; PTHR12992; PTHR12992; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS01293; NUDIX_COA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Metal-binding.
FT   CHAIN           1..192
FT                   /note="Uncharacterized Nudix hydrolase NudL"
FT                   /id="PRO_1000147826"
FT   DOMAIN          29..160
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
FT   MOTIF           67..89
FT                   /note="Nudix box"
FT   BINDING         83
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
FT   BINDING         87
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
SQ   SEQUENCE   192 AA;  21413 MW;  428D03827DF15F1D CRC64;
     MDTSRLTLDH FLSRFQLLRP QITHETLNQR QAAVLIPVVR RPQPGLLLTQ RAIHLRKHAG
     QVAFPGGAVD STDASLIAAA LREAQEEVAI PPQAVEVIGV LPPVDSVTGF QVTPVVGIIP
     PNLPWRASED EVSAVFEMPL AQALQLGRYH PLDVYRRGNS HRVWLSWYEH YFVWGMTANI
     LRELALQIGV KP