ID   CITG_ECOUT              Reviewed;         292 AA.
AC   Q1REU9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase {ECO:0000255|HAMAP-Rule:MF_00397};
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase {ECO:0000255|HAMAP-Rule:MF_00397};
DE            EC=2.4.2.52 {ECO:0000255|HAMAP-Rule:MF_00397};
GN   Name=citG {ECO:0000255|HAMAP-Rule:MF_00397}; OrderedLocusNames=UTI89_C0615;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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:0000255|HAMAP-Rule:MF_00397}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00397};
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00397}.
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DR   EMBL; CP000243; ABE06115.1; -; Genomic_DNA.
DR   RefSeq; WP_000062481.1; NC_007946.1.
DR   AlphaFoldDB; Q1REU9; -.
DR   EnsemblBacteria; ABE06115; ABE06115; UTI89_C0615.
DR   KEGG; eci:UTI89_C0615; -.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; QSWQRPA; -.
DR   Proteomes; UP000001952; 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_0000255401"
SQ   SEQUENCE   292 AA;  31662 MW;  DCC54A963ED82B9D CRC64;
     MSMPATSTKT TKLATSLIDE YALLGWRAML TEVNLSPKPG LVDRINCGAH KDMALEDFHR
     SALAIQGWLP RFIEFGACSA EMAPEEVLHG LRPIGMACEG DMFRATAGVN THKGSIFSLG
     LLCAAIGRLL QLNQSVTPIT ICATAASFCR GLTDRELRTN NSQLTAGQRL YQQLGLTGAR
     GEAEAGYPLV INHALPHYLT LLDQGLDPEL ALLDTLLLLM ATNGDTNVAS RGGEGGLRWL
     QREAQTLLNN GGIRTPADLD YLRQFDRECI ERNISPGGSA DLLILTWFLA QI