ID   CITX_ECOL5              Reviewed;         183 AA.
AC   Q0TK58;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=ECP_0645;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(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; CP000247; ABG68673.1; -; Genomic_DNA.
DR   RefSeq; WP_000550407.1; NC_008253.1.
DR   AlphaFoldDB; Q0TK58; -.
DR   SMR; Q0TK58; -.
DR   STRING; 362663.ECP_0645; -.
DR   EnsemblBacteria; ABG68673; ABG68673; ECP_0645.
DR   KEGG; ecp:ECP_0645; -.
DR   HOGENOM; CLU_104529_1_1_6; -.
DR   OMA; CGRSRKH; -.
DR   Proteomes; UP000009182; 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_1000049602"
SQ   SEQUENCE   183 AA;  20228 MW;  353DAB41BC78CBCE CRC64;
     MHLLPELASH HAVSIPELLV SRDERQARQH AWLKRHPVPL VSFTVVAPGP IKDSEVTRRI
     FNHGVTALRA LAAKQGWQIQ EQAALVSASG PEGMLSIAAP ARDLKLATIE LEHSHPLGRL
     WDIDVLTPEG DILSRRDYSL PPRRCLLCEQ SAAVCARGKT HQLTDLLNRM EALLNDVDAC
     NVN