ID   YFCD_ECOL6              Reviewed;         180 AA.
AC   P65557; P76494;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Uncharacterized Nudix hydrolase YfcD;
DE            EC=3.6.-.-;
GN   Name=yfcD; OrderedLocusNames=c2842;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN81296.1; -; Genomic_DNA.
DR   RefSeq; WP_000437935.1; NC_004431.1.
DR   AlphaFoldDB; P65557; -.
DR   SMR; P65557; -.
DR   STRING; 199310.c2842; -.
DR   EnsemblBacteria; AAN81296; AAN81296; c2842.
DR   GeneID; 67416729; -.
DR   KEGG; ecc:c2842; -.
DR   eggNOG; COG1443; Bacteria.
DR   HOGENOM; CLU_060552_3_0_6; -.
DR   OMA; PGYWDVA; -.
DR   BioCyc; ECOL199310:C2842-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR024195; NUDIX_hydrolase_YfcD_pred.
DR   Pfam; PF00293; NUDIX; 1.
DR   PIRSF; PIRSF017340; Nudix_hydro; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..180
FT                   /note="Uncharacterized Nudix hydrolase YfcD"
FT                   /id="PRO_0000057078"
FT   DOMAIN          35..163
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           72..94
FT                   /note="Nudix box"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   180 AA;  20376 MW;  83FC88B71EF9D58B CRC64;
     MEQRRLASTE WVDIVNEENE VIAQASREQM RAQCLRHRAT YIVVHDGMGK ILVQRRTETK
     DFLPGMLDAT AGGVVQADEQ LLESARREAE EELGIAGVPF AEHGQFYFED KNCRVWGALF
     SCVSHGPFAL QEDEVSEVCW LTPEEITARC DEFTPDSLKA LALWMKRNAK NEAVETETAE