ID   CITX_ECOLC              Reviewed;         183 AA.
AC   B1IYJ2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=EcolC_3030;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000946; ACA78654.1; -; Genomic_DNA.
DR   RefSeq; WP_000550414.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IYJ2; -.
DR   SMR; B1IYJ2; -.
DR   KEGG; ecl:EcolC_3030; -.
DR   HOGENOM; CLU_104529_1_1_6; -.
DR   OMA; CGRSRKH; -.
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_1000080329"
SQ   SEQUENCE   183 AA;  20286 MW;  22B3643BDABE06C8 CRC64;
     MHLLPELASH HAVSIPELLV SRDERQARQH VWLKRHPVPL VSFTVVAPGP IKDCEVTRRI
     FNHGVTALRA LAAKQGWQIQ EQAALVSASG PEGMLSIAAP ARDLKLATIE LEHSHPLGRL
     WDIDVLTPEG EILSRRDYSL PPRRCLLCEQ SAAVCARGKT HQLTDLLNRM EALLNDVDAC
     NVN