ID   CITX_VIBCH              Reviewed;         178 AA.
AC   Q9KTT8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Probable apo-citrate lyase phosphoribosyl-dephospho-CoA transferase;
DE            EC=2.7.7.61;
DE   AltName: Full=Apo-ACP nucleodityltransferase;
DE   AltName: Full=Holo-ACP synthase;
DE   AltName: Full=Holo-citrate lyase synthase;
GN   Name=citX; OrderedLocusNames=VC_0800;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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:0000250}.
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;
CC   -!- SIMILARITY: Belongs to the CitX family. {ECO:0000305}.
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DR   EMBL; AE003852; AAF93964.1; -; Genomic_DNA.
DR   PIR; B82278; B82278.
DR   RefSeq; NP_230449.1; NC_002505.1.
DR   RefSeq; WP_000018088.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KTT8; -.
DR   SMR; Q9KTT8; -.
DR   STRING; 243277.VC_0800; -.
DR   DNASU; 2615343; -.
DR   EnsemblBacteria; AAF93964; AAF93964; VC_0800.
DR   GeneID; 57739508; -.
DR   KEGG; vch:VC_0800; -.
DR   PATRIC; fig|243277.26.peg.763; -.
DR   eggNOG; COG3697; Bacteria.
DR   HOGENOM; CLU_104529_1_0_6; -.
DR   OMA; RNTMGVA; -.
DR   BioCyc; VCHO:VC0800-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
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; Reference proteome; Transferase.
FT   CHAIN           1..178
FT                   /note="Probable apo-citrate lyase phosphoribosyl-dephospho-
FT                   CoA transferase"
FT                   /id="PRO_0000214692"
SQ   SEQUENCE   178 AA;  20050 MW;  8B88A16570251994 CRC64;
     MSHHPDLSVS LDQLLLRKEV RVRQQGEWLK RHSLPLVSFT VNMPGAVKLN AASQTVMDAG
     MRAIQELCQK TGWRQVACQL LVEKTGPEAF VVIQAPSASM LKKAMMKIER EHPLGRLMDL
     DVIDVDGHII SRQGAQLPRR RCLLCERDAV ICARSRRHSV EALLAKIEEM THDYSCCA