ID   CITG_ECOL5              Reviewed;         292 AA.
AC   Q0TK59;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=ECP_0644;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(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; CP000247; ABG68672.1; -; Genomic_DNA.
DR   RefSeq; WP_000062470.1; NC_008253.1.
DR   AlphaFoldDB; Q0TK59; -.
DR   STRING; 362663.ECP_0644; -.
DR   EnsemblBacteria; ABG68672; ABG68672; ECP_0644.
DR   KEGG; ecp:ECP_0644; -.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; QSWQRPA; -.
DR   Proteomes; UP000009182; 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_0000255400"
SQ   SEQUENCE   292 AA;  31621 MW;  72BFC40249E35AF3 CRC64;
     MSMPATSTKT TKLATSLIDE YALLGWRAML TEVNLSPKPG LVDRINCGAH KDMALEDFHR
     SALAIQGWLP RFIEFGACSA EMAPEAVLNG LRPIGMACEG DMFRATAGVN THKGSIFSLG
     LLCAAIGRLL QLNQPVTPTT VCSTAASFCR GLTDRELRTN NARLTAGQRL YQQLGLTGAR
     GEAEAGYPLV INHALPHYLT LLDQGLDPEL ALLDTLLLLM ATNGDTNVAS RGGEGGLRWL
     QREAQTLLQK GGIRTPADLD YLRQFDRECI ERNLSPGGSA DLLILTWFLA QI