ID   CITX_SHIF8              Reviewed;         183 AA.
AC   Q0T702;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase;
DE            EC=2.7.7.61 {ECO:0000255|HAMAP-Rule:MF_00398};
DE   AltName: Full=Apo-ACP nucleodityltransferase {ECO:0000255|HAMAP-Rule:MF_00398};
DE   AltName: Full=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00398};
DE   AltName: Full=Holo-citrate lyase synthase {ECO:0000255|HAMAP-Rule:MF_00398};
GN   Name=citX {ECO:0000255|HAMAP-Rule:MF_00398}; OrderedLocusNames=SFV_0567;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
CC   -!- FUNCTION: Transfers 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A on
CC       a serine residue to the apo-acyl carrier protein (gamma chain) of the
CC       citrate lyase to yield holo-acyl carrier protein. {ECO:0000255|HAMAP-
CC       Rule:MF_00398}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00398};
CC   -!- SIMILARITY: Belongs to the CitX family. {ECO:0000255|HAMAP-
CC       Rule:MF_00398}.
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DR   EMBL; CP000266; ABF02824.1; -; Genomic_DNA.
DR   RefSeq; WP_000550399.1; NC_008258.1.
DR   AlphaFoldDB; Q0T702; -.
DR   SMR; Q0T702; -.
DR   EnsemblBacteria; ABF02824; ABF02824; SFV_0567.
DR   GeneID; 58390767; -.
DR   KEGG; sfv:SFV_0567; -.
DR   HOGENOM; CLU_104529_1_1_6; -.
DR   OMA; CGRSRKH; -.
DR   BioCyc; SFLE373384:SFV_RS03140-MON; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0050519; F:holo-citrate lyase synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051191; P:prosthetic group biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00398; CitX; 1.
DR   InterPro; IPR005551; CitX.
DR   Pfam; PF03802; CitX; 1.
DR   TIGRFAMs; TIGR03124; citrate_citX; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..183
FT                   /note="Apo-citrate lyase phosphoribosyl-dephospho-CoA
FT                   transferase"
FT                   /id="PRO_1000049604"
SQ   SEQUENCE   183 AA;  20352 MW;  CE28B0E0167A7B66 CRC64;
     MHLLPELASH HAVSIPELLV SRDERQARQH AWLKHHPVPL VSFTVVAPGP IKDSEVTRRI
     FNHRVTALRA LATKQGWQIQ EQAALVSASG PEGMLSIAAP ARDLKLATIE LEHSHPLGRL
     WDIDVLTPEG EILSRRDYSL PPRRCLLCEQ SAAVCARGKT HQLTDLLNRM EALLNDVDAC
     NVN