ID   NUDL_SALNS              Reviewed;         192 AA.
AC   B4SUL8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
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};
GN   OrderedLocusNames=SNSL254_A1965;
OS   Salmonella newport (strain SL254).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=423368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL254;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001113; ACF62493.1; -; Genomic_DNA.
DR   RefSeq; WP_000381549.1; NZ_CCMR01000003.1.
DR   AlphaFoldDB; B4SUL8; -.
DR   SMR; B4SUL8; -.
DR   EnsemblBacteria; ACF62493; ACF62493; SNSL254_A1965.
DR   KEGG; see:SNSL254_A1965; -.
DR   HOGENOM; CLU_040940_5_2_6; -.
DR   OMA; YYIWGAT; -.
DR   Proteomes; UP000008824; 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_1000147825"
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;  21430 MW;  BF9282892B51814E CRC64;
     MDTSRLTLNH FLSRFQLLRP QMTHETLNQR QAAVLIPVVR RPQPGLLLTQ RAIHLRKHAG
     QVAFPGGAVD STDASLIAAA LREAQEEVAI PPQAVEVIGV LPPVDSVTGF QVTPVVGIIP
     PNLPWRASED EVSAVFEMPL AQALQLGRYH PLDVYRRGNS HRVWLSWYEH YFVWGMTANI
     LRELALQIGV KP