ID   CITX_ECOUT              Reviewed;         183 AA.
AC   Q1REU8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=UTI89_C0616;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE06116.1; -; Genomic_DNA.
DR   RefSeq; WP_000550390.1; NC_007946.1.
DR   AlphaFoldDB; Q1REU8; -.
DR   SMR; Q1REU8; -.
DR   EnsemblBacteria; ABE06116; ABE06116; UTI89_C0616.
DR   KEGG; eci:UTI89_C0616; -.
DR   HOGENOM; CLU_104529_1_1_6; -.
DR   OMA; CGRSRKH; -.
DR   Proteomes; UP000001952; 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_1000049603"
SQ   SEQUENCE   183 AA;  20292 MW;  6286C14BA1690764 CRC64;
     MHLLPEFASH HAVSIPELLV SRDERQARQH AWLKRHPVPL VSFTVVAPGP IKDSEVTRRI
     FNHGVTALRA LATKQGWQIQ EQAALVSASG PEGMLSIAAP ARDLKLATIE LEHSHPLGRL
     WDIDVLTPEG DILSRRDYSL PPRRCLLCEQ SAAVCARGKT HQLTDLLNRM EALLNDVDAC
     NVN