(data stored in ACNUC7421 zone)

SWISSPROT: 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   05-JUL-2017, entry version 67.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Transfers 2-(5''-triphosphoribosyl)-3'-
CC       dephosphocoenzyme-A on a serine residue to the apo-acyl carrier
CC       protein (gamma chain) of the citrate lyase to yield holo-acyl
CC       carrier protein.
CC   -!- CATALYTIC ACTIVITY: 2'-(5-triphosphoribosyl)-3'-dephospho-CoA +
CC       citrate lyase apo-[acyl-carrier protein] = citrate lyase holo-
CC       [acyl-carrier protein] + diphosphate.
CC   -!- SIMILARITY: Belongs to the CitX family. {ECO:0000305}.
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_MWVM01000011.1.
DR   ProteinModelPortal; P0A6G6; -.
DR   STRING; 155864.Z0758; -.
DR   EnsemblBacteria; AAG54949; AAG54949; Z0758.
DR   EnsemblBacteria; BAB34076; BAB34076; BAB34076.
DR   GeneID; 917013; -.
DR   KEGG; ece:Z0758; -.
DR   KEGG; ecs:ECs0653; -.
DR   PATRIC; fig|386585.9.peg.764; -.
DR   eggNOG; ENOG4105YGP; Bacteria.
DR   eggNOG; COG3697; LUCA.
DR   HOGENOM; HOG000130710; -.
DR   KO; K05964; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0050519; F:holo-citrate lyase synthase activity; IEA:UniProtKB-EC.
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;
DR   PRODOM; P0A6G6.
DR   SWISS-2DPAGE; P0A6G6.
KW   Complete proteome; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    183       Apo-citrate lyase phosphoribosyl-
FT                                dephospho-CoA transferase.
FT                                /FTId=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
//

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