ID   CITX_VIBC3              Reviewed;         178 AA.
AC   A5F3C5; C3LYG8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Probable apo-citrate lyase phosphoribosyl-dephospho-CoA transferase {ECO:0000255|HAMAP-Rule:MF_00398};
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};
GN   OrderedLocusNames=VC0395_A0327, VC395_0817;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ20796.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP08834.1; -; Genomic_DNA.
DR   RefSeq; WP_000018079.1; NZ_JAACZH010000017.1.
DR   AlphaFoldDB; A5F3C5; -.
DR   SMR; A5F3C5; -.
DR   STRING; 345073.VC395_0817; -.
DR   EnsemblBacteria; ABQ20796; ABQ20796; VC0395_A0327.
DR   KEGG; vco:VC0395_A0327; -.
DR   KEGG; vcr:VC395_0817; -.
DR   PATRIC; fig|345073.21.peg.789; -.
DR   eggNOG; COG3697; Bacteria.
DR   HOGENOM; CLU_104529_1_0_6; -.
DR   OMA; RNTMGVA; -.
DR   Proteomes; UP000000249; Chromosome 2.
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..178
FT                   /note="Probable apo-citrate lyase phosphoribosyl-dephospho-
FT                   CoA transferase"
FT                   /id="PRO_1000072237"
SQ   SEQUENCE   178 AA;  20098 MW;  8B9CF16A203E1994 CRC64;
     MSHHPDLSVS LDQLLLRKEV RVRQQGEWLK RHSLPLVSFT VNMPGAFKLN AASQTVMDAG
     MRAIQELCQK TGWRQVACQL LVEKTGPEAF VVIQAPSASM LKKAMMKIER EHPLGRLMDL
     DVIDVDGHII SRQGAQLPRR RCLLCERDAV ICARSRRHSV EALLAKIEEM THDYSCCA