ID   CITG_SALAR              Reviewed;         298 AA.
AC   A9MKG0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Probable 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=SARI_02316;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX22179.1; -; Genomic_DNA.
DR   RefSeq; WP_000987082.1; NC_010067.1.
DR   AlphaFoldDB; A9MKG0; -.
DR   STRING; 41514.SARI_02316; -.
DR   EnsemblBacteria; ABX22179; ABX22179; SARI_02316.
DR   KEGG; ses:SARI_02316; -.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; MLTPKPG; -.
DR   OrthoDB; 1738403at2; -.
DR   Proteomes; UP000002084; 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; Reference proteome; Transferase.
FT   CHAIN           1..298
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase"
FT                   /id="PRO_1000080328"
SQ   SEQUENCE   298 AA;  32700 MW;  26EE73E2A413C1D6 CRC64;
     MMSIPVNPTN ASIQPQSLYD AWADLAWRAM LTEVNLSPKP GLVDRLNCGA HKDMALEDFH
     RSAEAIRDWL PRFMEYGASC TRLPPESVLA GLRPLGMACE AAMFRATAGV NTHKGSIFSL
     GLLCAAIGRL YQLRQPITAQ TLCATSAAFC RGLTARELRQ NNLQLTAGQR LYQQLGLTGA
     RGEAEAGYPL VIRHALPHYR ALLAQGRDPE LALLDTLLLL MSLNGDTNVA SRGGSDGLRW
     LQQHASFLLR QGGIRTPDDL VYLHQFNQQC IERNLSPGGS ADLLIVTWFL AQISQVNH