ID   CITXG_LEUMC             Reviewed;         467 AA.
AC   O53080;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 74.
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   Leuconostoc mesenteroides subsp. cremoris.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=33965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=195;
RX   PubMed=9457870; DOI=10.1128/jb.180.3.647-654.1998;
RA   Bekal S., van Beeumen J., Samyn B., Garmyn D., Henini S., Divies C.,
RA   Prevost H.;
RT   "Purification of Leuconostoc mesenteroides citrate lyase and cloning and
RT   characterization of the citCDEFG gene cluster.";
RL   J. Bacteriol. 180:647-654(1998).
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; Y10621; CAA71634.1; -; Genomic_DNA.
DR   AlphaFoldDB; O53080; -.
DR   SMR; O53080; -.
DR   PRIDE; O53080; -.
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; Transferase.
FT   CHAIN           1..467
FT                   /note="Protein CitXG"
FT                   /id="PRO_0000214683"
FT   REGION          1..178
FT                   /note="Apo-citrate lyase phosphoribosyl-dephospho-CoA
FT                   transferase"
FT   REGION          179..467
FT                   /note="2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A
FT                   synthase"
SQ   SEQUENCE   467 AA;  52012 MW;  0515A6063E4ACEA8 CRC64;
     MDYFEGGERL NLMQVLDNRE WREKYQKQLM ASFPTAVITS VKLNLPGPIK TSPKLQSVFQ
     IIINDLNPVF KDLQIIKEAS FVDQITGPDI FFVTSGCLKL VKQIMITFEE SHLLGRLLDL
     DVMCQNADKQ LSREELGFAP RKCLLCGKDA KTCIKEGNHS LAEGYSQINK MLHNFEKSKM
     IVPQMTQSQV VNAALTGMLY EVSLAPKPGL VDPSSNGAHK DMTVFTFIDS SLALQPYLNE
     AYRIGNQFKG TDLPRMFSLL RNAGIRAEKD MFAATNGVNT HKGAVFSLGI MVTAVAYATQ
     KGITNLLTIQ KVISDMTQDL VKNDLGKNNL RHSQNQQTAG ERQFIKYKIP GVRGEAEKGF
     PIVMNLALPF LCEQQGNLNQ RLLNTLMKIA GNIDDTNLIK RAGNATISKD MQHWSVTFFQ
     IGGSYTPEGL KFLNDLDQMF IKRNLSMGGA ADNLILTIFL ARLVGSL