ID   NUDL_YERPA              Reviewed;         199 AA.
AC   Q1C8W1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=YPA_1144;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG13111.1; -; Genomic_DNA.
DR   RefSeq; WP_002211080.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1C8W1; -.
DR   SMR; Q1C8W1; -.
DR   EnsemblBacteria; ABG13111; ABG13111; YPA_1144.
DR   GeneID; 66841918; -.
DR   KEGG; ypa:YPA_1144; -.
DR   OMA; YYIWGAT; -.
DR   Proteomes; UP000001971; 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..199
FT                   /note="Uncharacterized Nudix hydrolase NudL"
FT                   /id="PRO_0000315590"
FT   DOMAIN          38..169
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
FT   MOTIF           76..98
FT                   /note="Nudix box"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01592"
SQ   SEQUENCE   199 AA;  22244 MW;  0BE0B6BCD9B09F12 CRC64;
     MSELITGQYL SEFINRFQLQ LPQPDNVLTH SHYFSATNRR AAVLIPIICR PEPTLLLTRR
     ADHLRKHAGQ VAFPGGKADP DDQSLISTAL REAEEEVAIP ASVVHVLGKL APLNSSSGYH
     VTPIVGLVPA NIPFYGNDEE VAGLFEIPLH EALSLSRYHS LDIHREGINH RVYLSWYENQ
     FIWGLTATII RHLAQQVSI