ID   CITG2_SALTI             Reviewed;         298 AA.
AC   Q8Z8J2; Q7C8J2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase 2 {ECO:0000255|HAMAP-Rule:MF_00397};
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase 2 {ECO:0000255|HAMAP-Rule:MF_00397};
DE            EC=2.4.2.52 {ECO:0000255|HAMAP-Rule:MF_00397};
GN   Name=citG2 {ECO:0000255|HAMAP-Rule:MF_00397};
GN   OrderedLocusNames=STY0668, t2248;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD05096.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69850.1; -; Genomic_DNA.
DR   RefSeq; NP_455196.1; NC_003198.1.
DR   RefSeq; WP_000982670.1; NZ_WSUR01000015.1.
DR   AlphaFoldDB; Q8Z8J2; -.
DR   STRING; 220341.16501871; -.
DR   EnsemblBacteria; AAO69850; AAO69850; t2248.
DR   KEGG; stt:t2248; -.
DR   KEGG; sty:STY0668; -.
DR   PATRIC; fig|220341.7.peg.669; -.
DR   eggNOG; COG1767; Bacteria.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; QSWQRPA; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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..298
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase 2"
FT                   /id="PRO_0000255412"
SQ   SEQUENCE   298 AA;  32624 MW;  E2C2A5355E831530 CRC64;
     MMPIPVNPTN ASIQPQSLYD AWADLAWRAM LTEVNLSPKP GLVDRLNCGA HKDMALADFH
     RSAEAIRHWL PRFMEYGASC TRLPPESVLA GLRPLGMACE AAMFRATAGV NTHKGSIFSL
     GLLCAAIGRL YQLRQPIAAE TLCATAADFC RGLTTRELRQ NNLQLTAGQR LYQQLGLTGA
     RGEAEAGYPL VIRHALPHYR ALLAQGRDPE LALLDTLLLL MSLNGDTNVA SRGGADGLRW
     LQQQAAVLLH QGGIRTPDDL VYLHRFDQQC IERNLSPGGS ADLLIVTWFL AQISQVNH