CITX_ECO57
ID CITX_ECO57 Reviewed; 183 AA.
AC P0A6G6; P77563;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=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=Z0758, ECs0653;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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.
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; AE005174; AAG54949.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34076.1; -; Genomic_DNA.
DR PIR; E90710; E90710.
DR RefSeq; NP_308680.1; NC_002695.1.
DR RefSeq; WP_000550422.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A6G6; -.
DR SMR; P0A6G6; -.
DR STRING; 155864.EDL933_0687; -.
DR EnsemblBacteria; AAG54949; AAG54949; Z0758.
DR EnsemblBacteria; BAB34076; BAB34076; ECs_0653.
DR GeneID; 917013; -.
DR KEGG; ece:Z0758; -.
DR KEGG; ecs:ECs_0653; -.
DR PATRIC; fig|386585.9.peg.764; -.
DR eggNOG; COG3697; Bacteria.
DR HOGENOM; CLU_104529_1_1_6; -.
DR OMA; CGRSRKH; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Transferase.
FT CHAIN 1..183
FT /note="Apo-citrate lyase phosphoribosyl-dephospho-CoA
FT transferase"
FT /id="PRO_0000214686"
SQ SEQUENCE 183 AA; 20270 MW; 22BC3420DABE06D3 CRC64;
MHLLPELASH HAVSIPELLV SRDERQARQH VWLKRHPVPL VSFTVVAPGP IKDSEVTRRI
FNHGVTALRA LAAKQGWQIQ EQAALVSASG PEGMLSIAAP ARDLKLATIE LEHSHPLGRL
WDIDVLTPEG EILSRRDYSL PPRRCLLCEQ SAAVCARGKT HQLTDLLNRM EALLNDVDAC
NVN