ID   NUDL_KLEAE              Reviewed;         120 AA.
AC   P43338;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Uncharacterized Nudix hydrolase NudL;
DE            EC=3.6.1.-;
DE   Flags: Fragment;
GN   Name=nudL;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3057324; DOI=10.1093/oxfordjournals.molbev.a040512;
RA   Goncharoff P., Nichols B.P.;
RT   "Evolution of aminobenzoate synthases: nucleotide sequences of Salmonella
RT   typhimurium and Klebsiella aerogenes pabB.";
RL   Mol. Biol. Evol. 5:531-548(1988).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA   Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT   "Detection of new genes in a bacterial genome using Markov models for three
RT   gene classes.";
RL   Nucleic Acids Res. 23:3554-3562(1995).
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; M22078; AAA88208.1; -; Genomic_DNA.
DR   AlphaFoldDB; P43338; -.
DR   SMR; P43338; -.
DR   STRING; 548.EAG7_00980; -.
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: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; 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; PS01293; NUDIX_COA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Metal-binding.
FT   CHAIN           1..>120
FT                   /note="Uncharacterized Nudix hydrolase NudL"
FT                   /id="PRO_0000057146"
FT   DOMAIN          29..120
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           67..89
FT                   /note="Nudix box"
FT   BINDING         83
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   NON_TER         120
SQ   SEQUENCE   120 AA;  12797 MW;  E5D3D2512C44DBF8 CRC64;
     MADSALELDD FLSRFQLLRP QPHAPPLNQR QAAVLVPIVR RPQPGLLLTQ RSPLMRKHAG
     QVAFPGGAVD NSDATLIAAA LREAQEEVAI PPESVEVIGV LPPVDSVTGF QVTPVVGIIP