ID   CITXG_WEIPA             Reviewed;         462 AA.
AC   Q9RLT3;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Protein CitXG;
DE   Includes:
DE     RecName: Full=Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase;
DE              EC=2.7.7.61;
DE     AltName: Full=Apo-ACP nucleodityltransferase;
DE     AltName: Full=Holo-ACP synthase;
DE     AltName: Full=Holo-citrate lyase synthase;
DE   Includes:
DE     RecName: Full=2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase;
DE              Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase;
DE              EC=2.4.2.52;
GN   Name=citXG; Synonyms=citG;
OS   Weissella paramesenteroides (Leuconostoc paramesenteroides).
OG   Plasmid pCITJ1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Weissella.
OX   NCBI_TaxID=1249;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=J1;
RX   PubMed=10339813; DOI=10.1111/j.1574-6968.1999.tb13573.x;
RA   Martin M., Corrales M., de Mendoza D., Lopez P., Magni C.;
RT   "Cloning and molecular characterization of the citrate utilization
RT   citMCDEFGRP cluster of Leuconostoc paramesenteroides.";
RL   FEMS Microbiol. Lett. 174:231-238(1999).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes formation of 2-(5''-
CC       triphosphoribosyl)-3'-dephosphocoenzyme-A, and then the transfer of
CC       this prosthetic group precursor to the apo-acyl carrier protein (gamma
CC       chain) of the citrate lyase to yield the holo-acyl carrier protein.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + apo-
CC         [citrate lyase ACP] = diphosphate + holo-[citrate lyase ACP];
CC         Xref=Rhea:RHEA:16333, Rhea:RHEA-COMP:10157, Rhea:RHEA-COMP:10158,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:61378,
CC         ChEBI:CHEBI:82683; EC=2.7.7.61;
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   -!- SIMILARITY: In the N-terminal section; belongs to the CitX family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the CitG/MdcB family.
CC       {ECO:0000305}.
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DR   EMBL; AJ132782; CAB60044.1; -; Genomic_DNA.
DR   PIR; T46732; T46732.
DR   AlphaFoldDB; Q9RLT3; -.
DR   SMR; Q9RLT3; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050519; F:holo-citrate lyase synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   GO; GO:0051191; P:prosthetic group biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00397; CitG; 1.
DR   HAMAP; MF_00398; CitX; 1.
DR   InterPro; IPR002736; CitG.
DR   InterPro; IPR005551; CitX.
DR   InterPro; IPR017551; TriPribosyl-deP-CoA_syn_CitG.
DR   PANTHER; PTHR30201; PTHR30201; 1.
DR   Pfam; PF01874; CitG; 1.
DR   Pfam; PF03802; CitX; 1.
DR   TIGRFAMs; TIGR03125; citrate_citG; 1.
DR   TIGRFAMs; TIGR03124; citrate_citX; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Plasmid; Transferase.
FT   CHAIN           1..462
FT                   /note="Protein CitXG"
FT                   /id="PRO_0000214684"
FT   REGION          1..178
FT                   /note="Apo-citrate lyase phosphoribosyl-dephospho-CoA
FT                   transferase"
FT   REGION          179..462
FT                   /note="2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A
FT                   synthase"
SQ   SEQUENCE   462 AA;  51206 MW;  1302B481521FC4A5 CRC64;
     MSIFDIGEAV DLLTVLDNRE WRSRLQDKLK VTNSDKIVIS AKLNIPGPIK NNDILQKIFM
     DGWQTFVAGF ECNSQYEMLF AERATGPEAF ITVDGNLAAV KKTAILFEET YALGRLFDID
     VMANGQADYQ LSREDLGFGP RLCLICGKPA KVCAKEQNHT LDEGYEVINQ MYQGATSKEL
     IFEKESQETV VNNALKGLLY EVSLNPKPGL VDPVSMGSHT DMNMFMFIDS SLSLKSYLDK
     AFKLGRNFEG SDLKLLFNAL RAEGVLAEQT MFNATNNANT HKGAIFSLGI WVTAIAYSTK
     DGSATMTEVR RVIQRMVEGL IEKDLASNRV ATTAGEQQFQ TYQLTGIRGE AVNGFPGVSE
     VAVPFLQATF GTMTQRLLDT LMKIAATLED STLIKRAKTP DVLAEMKEWT SIYFKLGGSH
     TEQGMKYLYD LDRLFIERNL SIGGSADTLI LTIFIGQLTG LL