(data stored in ACNUC7421 zone)

SWISSPROT: NAGD_ECO57

ID   NAGD_ECO57              Reviewed;         250 AA.
AC   P0AF25; P15302;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   05-JUL-2017, entry version 75.
DE   RecName: Full=Ribonucleotide monophosphatase NagD;
DE            EC=3.1.3.5;
GN   Name=nagD; OrderedLocusNames=Z0822, ECs0705;
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of an unusually broad
CC       range of substrate including deoxyribo- and ribonucleoside tri-,
CC       di-, and monophosphates, as well as polyphosphate and glucose-1-P
CC       (Glu1P). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
CC       + phosphate.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Magnesium. Can also use other divalent metal cations as
CC       manganese, cobalt or zinc. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- INDUCTION: By N-acetylglucosamine. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD
CC       family. {ECO:0000305}.
DR   EMBL; AE005174; AAG54997.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34128.1; -; Genomic_DNA.
DR   PIR; A85567; A85567.
DR   PIR; A90717; A90717.
DR   RefSeq; NP_308732.1; NC_002695.1.
DR   RefSeq; WP_000153129.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; P0AF25; -.
DR   SMR; P0AF25; -.
DR   STRING; 155864.Z0822; -.
DR   EnsemblBacteria; AAG54997; AAG54997; Z0822.
DR   EnsemblBacteria; BAB34128; BAB34128; BAB34128.
DR   GeneID; 917074; -.
DR   KEGG; ece:Z0822; -.
DR   KEGG; ecs:ECs0705; -.
DR   PATRIC; fig|386585.9.peg.817; -.
DR   eggNOG; ENOG4105D4U; Bacteria.
DR   eggNOG; COG0647; LUCA.
DR   HOGENOM; HOG000068105; -.
DR   KO; K02566; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0008253; F:5'-nucleotidase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0AF25.
DR   SWISS-2DPAGE; P0AF25.
KW   Carbohydrate metabolism; Complete proteome; Hydrolase; Magnesium;
KW   Metal-binding.
FT   CHAIN         1    250       Ribonucleotide monophosphatase NagD.
FT                                /FTId=PRO_0000096695.
FT   REGION       42     43       Substrate binding. {ECO:0000250}.
FT   REGION      202    205       Substrate binding. {ECO:0000250}.
FT   ACT_SITE     11     11       {ECO:0000250}.
FT   METAL         9      9       Magnesium. {ECO:0000250}.
FT   METAL        11     11       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       201    201       Magnesium. {ECO:0000250}.
FT   BINDING      11     11       Substrate. {ECO:0000250}.
FT   BINDING     176    176       Substrate. {ECO:0000250}.
FT   SITE         55     55       Orients the Asp-11 for proton transfer
FT                                during catalytic turnover. {ECO:0000250}.
FT   SITE        146    146       Confers substrate specificity.
FT                                {ECO:0000250}.
SQ   SEQUENCE   250 AA;  27163 MW;  CC256AE6FF58DEBA CRC64;
     MTIKNVICDI DGVLMHDNVA VPGAAEFLHG IMDKGLPLVL LTNYPSQTGQ DLANRFATAG
     VDVPDSVFYT SAMATADFLR RQEGKKAYVV GEGALIHELY KAGFTITDVN PDFVIVGETR
     SYNWDMMHKA AYFVANGARF IATNPDTHGR GFYPACGALC AGIEKISGRK PFYVGKPSPW
     IIRAALNKMQ AHSEETVIVG DNLRTDILAG FQAGLETILV LSGVSSLDDI DSMPFRPSWI
     YPSVAEIDVI
//

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