ID   CITG_PHOPR              Reviewed;         314 AA.
AC   Q6LPV0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=PBPRA2290;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(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; CR378670; CAG20676.1; -; Genomic_DNA.
DR   RefSeq; WP_011218965.1; NC_006370.1.
DR   AlphaFoldDB; Q6LPV0; -.
DR   STRING; 298386.PBPRA2290; -.
DR   EnsemblBacteria; CAG20676; CAG20676; PBPRA2290.
DR   KEGG; ppr:PBPRA2290; -.
DR   eggNOG; COG1767; Bacteria.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; MLTPKPG; -.
DR   OrthoDB; 1738403at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
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..314
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase"
FT                   /id="PRO_0000255402"
SQ   SEQUENCE   314 AA;  34528 MW;  4F1309EC88F74863 CRC64;
     MINSAVNLLV NPQDYYIKSE SREDLPQINL FKLVGNLGYH AMMLEVHLTP KPGLVDLCTN
     GAHDDMDIHT FENSAQAINP FLIKFLYAGL NHSDTPIDSL LPKLRPVGLN AEEAMFQATS
     GINTHKGMIF SLGIVCGVIG WLRGNNLSFD AMHISKAVKC CCHDLVFKEL RQNHDKPKTY
     GEFLYKEHGL TGARGEAASG LATVMDHGLP AFEKTVKEGF STEQALWQSL LVLMANNLDT
     NLVSRGGMEG LLYAQQAAQG LLVKGGCRYT NLESELTELD EIFTEKKLSP GGSADLLAIT
     WLLAQMNELS PKYV