ID   CITG1_SALPA             Reviewed;         302 AA.
AC   Q5PKJ2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=SPA0064;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76099.1; -; Genomic_DNA.
DR   RefSeq; WP_001103243.1; NC_006511.1.
DR   AlphaFoldDB; Q5PKJ2; -.
DR   EnsemblBacteria; AAV76099; AAV76099; SPA0064.
DR   KEGG; spt:SPA0064; -.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; MLTPKPG; -.
DR   Proteomes; UP000008185; 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_0000255409"
SQ   SEQUENCE   302 AA;  32950 MW;  F0D922B2B1DD132E CRC64;
     MNVSVVTERR TPAYSSLAAG ELNGLVARAL LTEARLTPKP GLVDIRNSGA HRDMDLAAFE
     RSTTAIAPWM EKFFIMGNNT AALAAENVLV MLRPLGMACE NDMLQATNGV NTHRRAIFAF
     GLLSAAIGRL LARGEPLEQN RICDQVARLS RNIVAHELSA KKAGKLTKSE THFQCYGLSG
     ARGEAESGFR TVRTQALPVF NRVVQEHDDT HLALLQTLLH LMAWNDDTNL VSRGGLEGLY
     YVQQQAQKLL WQGGVLVEGG IEAMQSLDDE LILRNLSPGG SADLLAVTWF LSHFPAGSLY
     PE