ID   MODD_ECO27              Reviewed;         284 AA.
AC   P94777; B7UQ81; O87502;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 4.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Putative pyrophosphorylase ModD;
DE            EC=2.4.2.-;
GN   Name=modD; OrderedLocusNames=E2348C_1316;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Haigh R.D., Willliams P.H.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- MISCELLANEOUS: Orthologs of this gene seem to exist only in pathogenic
CC       strains of E.coli but not in the K12 strain.
CC   -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
CC   -!- CAUTION: Was originally (Ref.1) thought to be involved in molybdate
CC       transport. {ECO:0000305}.
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DR   EMBL; U85771; AAB42092.1; -; Genomic_DNA.
DR   EMBL; FM180568; CAS08864.1; -; Genomic_DNA.
DR   RefSeq; WP_000576825.1; NC_011601.1.
DR   AlphaFoldDB; P94777; -.
DR   SMR; P94777; -.
DR   EnsemblBacteria; CAS08864; CAS08864; E2348C_1316.
DR   KEGG; ecg:E2348C_1316; -.
DR   HOGENOM; CLU_039622_2_1_6; -.
DR   OMA; GGHIHRQ; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.90.1170.20; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006242; ModD.
DR   InterPro; IPR027277; NadC/ModD.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR   InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR   InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR   PANTHER; PTHR32179; PTHR32179; 1.
DR   Pfam; PF01729; QRPTase_C; 1.
DR   Pfam; PF02749; QRPTase_N; 1.
DR   PIRSF; PIRSF006250; NadC_ModD; 1.
DR   SUPFAM; SSF51690; SSF51690; 1.
DR   TIGRFAMs; TIGR01334; modD; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..284
FT                   /note="Putative pyrophosphorylase ModD"
FT                   /id="PRO_0000155957"
FT   CONFLICT        104..126
FT                   /note="CGVSDYLAQMLALLRERYPDGNI -> LRLFLIISLKCWRYFVNVTLMAIF
FT                   (in Ref. 1; AAB42092)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="A -> P (in Ref. 1; AAB42092)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   284 AA;  30479 MW;  9FD9D765FBEC8F4B CRC64;
     MIFLSQAQID ALLLEDIQGG DLTTRALNIG HQHGYIEFFL RQGGCVSGIS VACKMLTTLG
     LTIDDAVSDG SQANAGQRLI RAQGNAAALH QGWKAVQNVL EWSCGVSDYL AQMLALLRER
     YPDGNIACTR KAIPGTRLLA SQAILAAGGL IHRAGCAETI LLFANHRHFL HDNQDWSGAI
     NQLRRHAPEK KIVVEADAPK EAIAALRAQP DVLQLDKFSP QQATEIAQIA PSLAPHCTLA
     LTGGINLTTL KNYLDCGIRL FITSAPYYAA PADIKVSLQP AASI