ID   NUDL_ECO24              Reviewed;         192 AA.
AC   A7ZMT6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=EcE24377A_2041;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV18449.1; -; Genomic_DNA.
DR   RefSeq; WP_000456740.1; NC_009801.1.
DR   AlphaFoldDB; A7ZMT6; -.
DR   SMR; A7ZMT6; -.
DR   EnsemblBacteria; ABV18449; ABV18449; EcE24377A_2041.
DR   KEGG; ecw:EcE24377A_2041; -.
DR   HOGENOM; CLU_040940_5_2_6; -.
DR   OMA; YYIWGAT; -.
DR   Proteomes; UP000001122; 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_0000315573"
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;  21512 MW;  F82B07BDBF4FFC24 CRC64;
     MEYRSLTLDY FLSRFQLLRP QINRETLNHR QAAVLIPIVR RPQPGLLLTQ RSIHLRKHAG
     QVAFPGGAVD DTDASVIAAA LREAEEEVAI PPSAVEVIGV LPPVDSVTGY QVTPVVGIIP
     PDLPYRASED EVSAVFEMPL AQALHLGRYH PLDIYRRGDS HRVWLSWYEQ YFVWGMTAGI
     IRELALQIGV KP