YFCD_ECO57
ID YFCD_ECO57 Reviewed; 180 AA.
AC P65558; P76494;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Uncharacterized Nudix hydrolase YfcD;
DE EC=3.6.-.-;
GN Name=yfcD; OrderedLocusNames=Z3561, ECs3183;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AE005174; AAG57428.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36606.1; -; Genomic_DNA.
DR PIR; G91026; G91026.
DR PIR; H85870; H85870.
DR RefSeq; NP_311210.1; NC_002695.1.
DR RefSeq; WP_000437935.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P65558; -.
DR SMR; P65558; -.
DR STRING; 155864.EDL933_3464; -.
DR EnsemblBacteria; AAG57428; AAG57428; Z3561.
DR EnsemblBacteria; BAB36606; BAB36606; ECs_3183.
DR GeneID; 67416729; -.
DR GeneID; 916891; -.
DR KEGG; ece:Z3561; -.
DR KEGG; ecs:ECs_3183; -.
DR PATRIC; fig|386585.9.peg.3323; -.
DR eggNOG; COG1443; Bacteria.
DR HOGENOM; CLU_060552_3_0_6; -.
DR OMA; PGYWDVA; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome.
FT CHAIN 1..180
FT /note="Uncharacterized Nudix hydrolase YfcD"
FT /id="PRO_0000057079"
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