ID   MODD_ECOL6              Reviewed;         284 AA.
AC   P59245;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Putative pyrophosphorylase ModD;
DE            EC=2.4.2.-;
GN   Name=modD; OrderedLocusNames=c1647;
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 [GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=9712795; DOI=10.1128/iai.66.9.4411-4417.1998;
RA   Guyer D.M., Kao J.-S., Mobley H.L.T.;
RT   "Genomic analysis of a pathogenicity island in uropathogenic Escherichia
RT   coli CFT073: distribution of homologous sequences among isolates from
RT   patients with pyelonephritis, cystitis, and catheter-associated bacteriuria
RT   and from fecal samples.";
RL   Infect. Immun. 66:4411-4417(1998).
RN   [2]
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   -!- 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}.
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DR   EMBL; AF081283; AAC61710.1; -; Genomic_DNA.
DR   EMBL; AE014075; AAN80112.1; -; Genomic_DNA.
DR   RefSeq; WP_000576827.1; NC_004431.1.
DR   AlphaFoldDB; P59245; -.
DR   SMR; P59245; -.
DR   STRING; 199310.c1647; -.
DR   EnsemblBacteria; AAN80112; AAN80112; c1647.
DR   KEGG; ecc:c1647; -.
DR   eggNOG; COG0157; Bacteria.
DR   HOGENOM; CLU_039622_2_1_6; -.
DR   OMA; GGHIHRQ; -.
DR   BioCyc; ECOL199310:C1647-MON; -.
DR   Proteomes; UP000001410; 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_0000155958"
FT   CONFLICT        104..126
FT                   /note="CGVSDYLAQMLALLRERYPDGNI -> LRLFLIISLKCWRYFVNVTLMAIF
FT                   (in Ref. 1; AAC61710)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   284 AA;  30509 MW;  6B889271BEEC9451 CRC64;
     MIFLSQAQID ALLLEDIQGG DLTTRALNIG HQHGYIEFFL RQGGCVSGIS VACKMLTTLG
     LTIDDAVSDG SQANAGQRLI RAQGNAAALH QGWKAVQNVL EWSCGVSDYL AQMLALLRER
     YPDGNIACTR KAIPGTRLLA SQAILAAGGL IHRAGCAETI LLFANHRHFL HDNQDWSGAI
     NQLRRHAPEK KIVVEADTPK EAIAALRAQP DVLQLDKFSP QQATEIAQIA PSLAPHCTLA
     LTGGINLTTL KNYLDCGIRL FITSAPYYAA PADIKVSLQP AASI