ID   CITG_ECOL6              Reviewed;         292 AA.
AC   Q8FK04;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase;
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase;
DE            EC=2.4.2.52;
GN   Name=citG; OrderedLocusNames=c0701;
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 [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   -!- FUNCTION: Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-
CC       dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-
CC       acyl carrier protein (gamma chain) of citrate lyase, from ATP and
CC       dephospho-CoA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-
CC         3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57328, ChEBI:CHEBI:61378; EC=2.4.2.52;
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN79176.1; -; Genomic_DNA.
DR   RefSeq; WP_000062478.1; NC_004431.1.
DR   AlphaFoldDB; Q8FK04; -.
DR   STRING; 199310.c0701; -.
DR   EnsemblBacteria; AAN79176; AAN79176; c0701.
DR   KEGG; ecc:c0701; -.
DR   eggNOG; COG1767; Bacteria.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; QSWQRPA; -.
DR   BioCyc; ECOL199310:C0701-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   HAMAP; MF_00397; CitG; 1.
DR   InterPro; IPR002736; CitG.
DR   InterPro; IPR017551; TriPribosyl-deP-CoA_syn_CitG.
DR   PANTHER; PTHR30201; PTHR30201; 1.
DR   Pfam; PF01874; CitG; 1.
DR   TIGRFAMs; TIGR03125; citrate_citG; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Transferase.
FT   CHAIN           1..292
FT                   /note="2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A
FT                   synthase"
FT                   /id="PRO_0000214665"
SQ   SEQUENCE   292 AA;  31581 MW;  2FB1A920B5A205D9 CRC64;
     MSMPATSTKT TKLATSLIDE YALLGWRAML TEVNLSPKPG LVDRINCGAH KDMALEDFHR
     SALAIQGWLP RFIEFGACSA EMAPEAVLNG LRPIGMACEG DMFRATAGVN THKGSIFSLG
     LLCAAIGRLL QLNQSVTPIT ICATAASFCR GLTDRELRTN NSQLTAGQRL YQQLGLTGAR
     GEAEAGYPLV INHALPHYLT LLDQGLDPEL ALLDTLLLLM ATNGDTNVAS RGGEGGLRWL
     QREAQTLLNN GGIRTPADLD YLRQFDRECI ERNISPGGSA DLLILTWFLA QI