ID   CITG2_SALTY             Reviewed;         298 AA.
AC   Q8ZR14;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 84.
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}; OrderedLocusNames=STM0619;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL19570.1; -; Genomic_DNA.
DR   RefSeq; NP_459611.1; NC_003197.2.
DR   RefSeq; WP_000982663.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZR14; -.
DR   STRING; 99287.STM0619; -.
DR   PaxDb; Q8ZR14; -.
DR   EnsemblBacteria; AAL19570; AAL19570; STM0619.
DR   GeneID; 1252139; -.
DR   KEGG; stm:STM0619; -.
DR   PATRIC; fig|99287.12.peg.652; -.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; QSWQRPA; -.
DR   PhylomeDB; Q8ZR14; -.
DR   BioCyc; SENT99287:STM0619-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   GO; GO:0051191; P:prosthetic group biosynthetic process; IBA:GO_Central.
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 2"
FT                   /id="PRO_0000255414"
SQ   SEQUENCE   298 AA;  32615 MW;  97C8BE8DE9581A5C CRC64;
     MMPIPANPTN ASIQPQSLYD VWADLAWRAM LTEVNLSPKP GLVDRLNCGA HKDMALADFH
     RSAEAIRHWL PRFMEYGASC TRLPPESVLA GLRPLGMACE AAMFRATAGV NTHKGSIFSL
     GLLCAAIGRL YQLRQPIAAE TLCATAADFC RGLTTRELRQ NNLQLTAGQR LYQQLGLTGA
     RGEAEAGYPL VIRHALPHYR ALLAQGRDPE LALLDTLLLL MSLNGDTNVA SRGGADGLRW
     LQQQAAVLLQ QGGIRTPDDL VYLHRFDQQC IERNLSPGGS ADLLIVTWFL AQISQVNH