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NUDL_ECO57
ID   NUDL_ECO57              Reviewed;         192 AA.
AC   Q8XCQ2; Q7AD94;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=Z2856, ECs2522;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG56802.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35945.1; -; Genomic_DNA.
DR   PIR; B90944; B90944.
DR   PIR; F85792; F85792.
DR   RefSeq; NP_310549.1; NC_002695.1.
DR   RefSeq; WP_000456725.1; NZ_SWKA01000004.1.
DR   AlphaFoldDB; Q8XCQ2; -.
DR   SMR; Q8XCQ2; -.
DR   STRING; 155864.EDL933_2783; -.
DR   EnsemblBacteria; AAG56802; AAG56802; Z2856.
DR   EnsemblBacteria; BAB35945; BAB35945; ECs_2522.
DR   GeneID; 66674298; -.
DR   GeneID; 912636; -.
DR   KEGG; ece:Z2856; -.
DR   KEGG; ecs:ECs_2522; -.
DR   PATRIC; fig|386585.9.peg.2643; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_040940_5_2_6; -.
DR   OMA; YYIWGAT; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome.
FT   CHAIN           1..192
FT                   /note="Uncharacterized Nudix hydrolase NudL"
FT                   /id="PRO_0000315574"
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;  21464 MW;  54CAFB50BF52F5A2 CRC64;
     MEYRSLTLDD FLSRFQLLRP QINRETLNHR QAAVLIPIVR RPQPGLLLTQ RSIHLRKHAG
     QVAFPGGAVD DTDASVIAAA LREAEEEVAI PPSAVEVIGV LPPVDSVTGY QVTPVVGIIP
     PDLPYRASED EVSAVFEMPL AQALHLGRYH PLDIYRRGDS HRVWLSWYEQ YFVWGMTAGI
     IRELALQIGV KP
 
 
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