YJJG_ECO57
ID YJJG_ECO57 Reviewed; 225 AA.
AC P0A8Y2; P33999; P76818;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Pyrimidine 5'-nucleotidase YjjG {ECO:0000250|UniProtKB:P0A8Y1};
DE EC=3.1.3.5 {ECO:0000250|UniProtKB:P0A8Y1};
DE AltName: Full=House-cleaning nucleotidase {ECO:0000250|UniProtKB:P0A8Y1};
DE AltName: Full=Non-canonical pyrimidine nucleotide phosphatase {ECO:0000250|UniProtKB:P0A8Y1};
DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase {ECO:0000250|UniProtKB:P0A8Y1};
DE AltName: Full=dUMP phosphatase {ECO:0000250|UniProtKB:P0A8Y1};
GN Name=yjjG; OrderedLocusNames=Z5975, ECs5332;
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: Nucleotidase that shows high phosphatase activity toward non-
CC canonical pyrimidine nucleotides and three canonical nucleoside 5'-
CC monophosphates (UMP, dUMP, and dTMP), and very low activity against
CC TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6-phosphogluconate. Appears to
CC function as a house-cleaning nucleotidase in vivo, since the general
CC nucleotidase activity of YjjG allows it to protect cells against non-
CC canonical pyrimidine derivatives such as 5-fluoro-2'-deoxyuridine, 5-
CC fluorouridine, 5-fluoroorotate, 5-fluorouracil, and 5-aza-2'-
CC deoxycytidine, and prevents the incorporation of potentially mutagenic
CC nucleotides into DNA. Its dUMP phosphatase activity that catalyzes the
CC hydrolysis of dUMP to deoxyuridine is necessary for thymine utilization
CC via the thymine salvage pathway. Is strictly specific to substrates
CC with 5'-phosphates and shows no activity against nucleoside 2'- or 3'-
CC monophosphates. {ECO:0000250|UniProtKB:P0A8Y1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000250|UniProtKB:P0A8Y1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-
CC deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:65317; Evidence={ECO:0000250|UniProtKB:P0A8Y1};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P0A8Y1};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A8Y1};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P0A8Y1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. YjjG family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG59554.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38755.1; -; Genomic_DNA.
DR PIR; D91295; D91295.
DR PIR; F86136; F86136.
DR RefSeq; NP_313359.1; NC_002695.1.
DR RefSeq; WP_000870710.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A8Y2; -.
DR SMR; P0A8Y2; -.
DR STRING; 155864.EDL933_5715; -.
DR PRIDE; P0A8Y2; -.
DR EnsemblBacteria; AAG59554; AAG59554; Z5975.
DR EnsemblBacteria; BAB38755; BAB38755; ECs_5332.
DR GeneID; 913547; -.
DR KEGG; ece:Z5975; -.
DR KEGG; ecs:ECs_5332; -.
DR PATRIC; fig|386585.9.peg.5576; -.
DR eggNOG; COG1011; Bacteria.
DR HOGENOM; CLU_045011_8_1_6; -.
DR OMA; DHTLWDF; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR011951; HAD-SF_hydro_IA_YjjG/PynA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR02254; YjjG/YfnB; 1.
PE 3: Inferred from homology;
KW Cobalt; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..225
FT /note="Pyrimidine 5'-nucleotidase YjjG"
FT /id="PRO_0000066273"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 225 AA; 25301 MW; D8A52E086567BA71 CRC64;
MKWDWIFFDA DETLFTFDSF TGLQRMFLDY SVTFTAEDFQ DYQAVNKPLW VDYQNGAITS
LQLQHGRFES WAERLNVEPG KLNEAFINAM AEICTPLPGA VSLLNAIRGN AKIGIITNGF
SALQQVRLER TGLRDYFDLL VISEEVGVAK PNKKIFDYAL EQAGNPDRSR VLMVGDTAES
DILGGINAGL ATCWLNAHHR EQPEGIAPTW TVSSLHELEQ LLCKH
