ID   CITG1_SALCH             Reviewed;         302 AA.
AC   Q57TJ8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase 1 {ECO:0000255|HAMAP-Rule:MF_00397};
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase 1 {ECO:0000255|HAMAP-Rule:MF_00397};
DE            EC=2.4.2.52 {ECO:0000255|HAMAP-Rule:MF_00397};
GN   Name=citG1 {ECO:0000255|HAMAP-Rule:MF_00397}; OrderedLocusNames=SCH_0057;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX63963.1; -; Genomic_DNA.
DR   RefSeq; WP_001103238.1; NC_006905.1.
DR   AlphaFoldDB; Q57TJ8; -.
DR   EnsemblBacteria; AAX63963; AAX63963; SCH_0057.
DR   KEGG; sec:SCH_0057; -.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; MLTPKPG; -.
DR   Proteomes; UP000000538; 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..302
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase 1"
FT                   /id="PRO_0000255407"
SQ   SEQUENCE   302 AA;  32851 MW;  ADA93ECBD4D47F57 CRC64;
     MNVSVVTERR TPAYSSLAAG ELNGLVARAL LTEARLTPKP GLVDIRNSGA HRDMDLAAFE
     RSTTAIAPWM EKFFIMGNNT AALAAENVLV MLRPLGMACE NDMLQATNGV NTHRGAIFAF
     GLLSAAIGRL LARGEPLEQN RICDQVARLS RNIVAHELSA KKAGKLTKSE THFQCYGLSG
     ARGEAESGFR TVRTQALPVF NRVVQEHDDT HLALLQTLLH LMAWNDDTNL VSRGGLEGLY
     YVQQQAQKLL WQGGVLVEGG IEAMQSLDDE LILRNLSPGG SADLLAVTWF LSHFPAGSLY
     PE