CITX_ECOLI
ID CITX_ECOLI Reviewed; 183 AA.
AC P0A6G5; P77563; Q2MBK2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase;
DE EC=2.7.7.61 {ECO:0000269|PubMed:10924139, ECO:0000269|PubMed:11042274};
DE AltName: Full=Apo-ACP nucleodityltransferase;
DE AltName: Full=Holo-ACP synthase;
DE AltName: Full=Holo-citrate lyase synthase;
GN Name=citX; Synonyms=ybdU; OrderedLocusNames=b0614, JW0606;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP GENE NAME.
RC STRAIN=K12;
RX PubMed=9696764; DOI=10.1128/jb.180.16.4160-4165.1998;
RA Pos K.M., Dimroth P., Bott M.;
RT "The Escherichia coli citrate carrier CitT: a member of a novel eubacterial
RT transporter family related to the 2-oxoglutarate/malate translocator from
RT spinach chloroplasts.";
RL J. Bacteriol. 180:4160-4165(1998).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11042274; DOI=10.1016/s0014-5793(00)02105-0;
RA Schneider K., Dimroth P., Bott M.;
RT "Identification of triphosphoribosyl-dephospho-CoA as precursor of the
RT citrate lyase prosthetic group.";
RL FEBS Lett. 483:165-168(2000).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=BL21-DE3, and K12 / DH5-alpha;
RX PubMed=10924139; DOI=10.1021/bi000401r;
RA Schneider K., Dimroth P., Bott M.;
RT "Biosynthesis of the prosthetic group of citrate lyase.";
RL Biochemistry 39:9438-9450(2000).
RN [7]
RP OPERON STRUCTURE, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=19429622; DOI=10.1128/jb.00108-09;
RA Shimada T., Yamamoto K., Ishihama A.;
RT "Involvement of the leucine response transcription factor LeuO in
RT regulation of the genes for sulfa drug efflux.";
RL J. Bacteriol. 191:4562-4571(2009).
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 {ECO:0000269|PubMed:10924139, ECO:0000269|PubMed:11042274}.
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 Evidence={ECO:0000269|PubMed:10924139, ECO:0000269|PubMed:11042274};
CC -!- INDUCTION: Repressed by H-NS. Part of the citCDEFXG operon.
CC {ECO:0000269|PubMed:19429622}.
CC -!- SIMILARITY: Belongs to the CitX family. {ECO:0000305}.
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DR EMBL; U82598; AAB40814.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73715.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76354.1; -; Genomic_DNA.
DR PIR; D64795; D64795.
DR RefSeq; NP_415147.1; NC_000913.3.
DR RefSeq; WP_000550422.1; NZ_STEB01000031.1.
DR AlphaFoldDB; P0A6G5; -.
DR SMR; P0A6G5; -.
DR BioGRID; 4260860; 9.
DR BioGRID; 853325; 2.
DR IntAct; P0A6G5; 8.
DR STRING; 511145.b0614; -.
DR PaxDb; P0A6G5; -.
DR PRIDE; P0A6G5; -.
DR EnsemblBacteria; AAC73715; AAC73715; b0614.
DR EnsemblBacteria; BAE76354; BAE76354; BAE76354.
DR GeneID; 949084; -.
DR KEGG; ecj:JW0606; -.
DR KEGG; eco:b0614; -.
DR PATRIC; fig|1411691.4.peg.1654; -.
DR EchoBASE; EB3310; -.
DR eggNOG; COG3697; Bacteria.
DR HOGENOM; CLU_104529_1_1_6; -.
DR InParanoid; P0A6G5; -.
DR OMA; CGRSRKH; -.
DR PhylomeDB; P0A6G5; -.
DR BioCyc; EcoCyc:G6340-MON; -.
DR BioCyc; MetaCyc:G6340-MON; -.
DR PRO; PR:P0A6G5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0050519; F:holo-citrate lyase synthase activity; IDA:EcoCyc.
DR GO; GO:0051191; P:prosthetic group biosynthetic process; IEA:InterPro.
DR GO; GO:0018247; P:protein-phosphoribosyl dephospho-coenzyme A linkage; IDA:EcoCyc.
DR HAMAP; MF_00398; CitX; 1.
DR InterPro; IPR005551; CitX.
DR Pfam; PF03802; CitX; 1.
DR TIGRFAMs; TIGR03124; citrate_citX; 1.
PE 1: Evidence at protein level;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..183
FT /note="Apo-citrate lyase phosphoribosyl-dephospho-CoA
FT transferase"
FT /id="PRO_0000214685"
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
