CITG_ECOLI
ID CITG_ECOLI Reviewed; 292 AA.
AC P77231; Q2MBK3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase;
DE Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase;
DE EC=2.4.2.52 {ECO:0000269|PubMed:11042274};
GN Name=citG; Synonyms=ybdT; OrderedLocusNames=b0613, JW0605;
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 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 [5]
RP FUNCTION.
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 [6]
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: Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-
CC dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-
CC acyl carrier protein (gamma chain) of citrate lyase, from ATP and
CC dephospho-CoA. {ECO:0000269|PubMed:10924139,
CC ECO:0000269|PubMed:11042274}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-
CC 3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57328, ChEBI:CHEBI:61378; EC=2.4.2.52;
CC Evidence={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 CitG/MdcB family. {ECO:0000305}.
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DR EMBL; U82598; AAB40813.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73714.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76353.1; -; Genomic_DNA.
DR PIR; C64795; C64795.
DR RefSeq; NP_415146.1; NC_000913.3.
DR RefSeq; WP_000062457.1; NZ_STEB01000031.1.
DR AlphaFoldDB; P77231; -.
DR BioGRID; 4259903; 8.
DR IntAct; P77231; 2.
DR STRING; 511145.b0613; -.
DR PaxDb; P77231; -.
DR PRIDE; P77231; -.
DR EnsemblBacteria; AAC73714; AAC73714; b0613.
DR EnsemblBacteria; BAE76353; BAE76353; BAE76353.
DR GeneID; 946395; -.
DR KEGG; ecj:JW0605; -.
DR KEGG; eco:b0613; -.
DR PATRIC; fig|1411691.4.peg.1655; -.
DR EchoBASE; EB3309; -.
DR eggNOG; COG1767; Bacteria.
DR HOGENOM; CLU_056179_1_0_6; -.
DR InParanoid; P77231; -.
DR OMA; QSWQRPA; -.
DR PhylomeDB; P77231; -.
DR BioCyc; EcoCyc:G6339-MON; -.
DR BioCyc; MetaCyc:G6339-MON; -.
DR BRENDA; 2.4.2.52; 2026.
DR PRO; PR:P77231; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IDA:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR GO; GO:0051191; P:prosthetic group biosynthetic process; IDA:EcoCyc.
DR HAMAP; MF_00397; CitG; 1.
DR InterPro; IPR002736; CitG.
DR InterPro; IPR017551; TriPribosyl-deP-CoA_syn_CitG.
DR PANTHER; PTHR30201; PTHR30201; 1.
DR Pfam; PF01874; CitG; 1.
DR TIGRFAMs; TIGR03125; citrate_citG; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..292
FT /note="2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A
FT synthase"
FT /id="PRO_0000214664"
SQ SEQUENCE 292 AA; 31644 MW; 0BE3C24BE33E0AE8 CRC64;
MSMPATSTKT TKLATSLIDE YALLGWRAML TEVNLSPKPG LVDRINCGAH KDMALEDFHR
SALAIQGWLP RFIEFGACSA EMAPEAVLHG LRPIGMACEG DMFRATAGVN THKGSIFSLG
LLCAAIGRLL QLNQPVTPTT VCSTAASFCR GLTDRELRTN NSQLTAGQRL YQQLGLTGAR
GEAEAGYPLV INHALPHYLT LLDQGLDPEL ALLDTLLLLM AINGDTNVAS RGGEGGLRWL
QREAQTLLQK GGIRTPADLD YLRQFDRECI ERNLSPGGSA DLLILTWFLA QI
