ID   F4NLK9_ECOLX            Unreviewed;       292 AA.
AC   F4NLK9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   04-FEB-2015, entry version 22.
DE   RecName: Full=2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase {ECO:0000256|HAMAP-Rule:MF_00397};
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase {ECO:0000256|HAMAP-Rule:MF_00397};
DE            EC=2.4.2.52 {ECO:0000256|HAMAP-Rule:MF_00397};
GN   Name=citG {ECO:0000256|HAMAP-Rule:MF_00397,
GN   ECO:0000313|EMBL:EGJ07448.1};
GN   ORFNames=SSJG_03498 {ECO:0000313|EMBL:EGJ07448.1};
OS   Escherichia coli D9.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=556266 {ECO:0000313|EMBL:EGJ07448.1};
RN   [1] {ECO:0000313|EMBL:EGJ07448.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=D9 {ECO:0000313|EMBL:EGJ07448.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T.,
RA   Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E.,
RA   Strauss J., Sibley C., White A., Ambrose C., Lander E., Nusbaum C.,
RA   Galagan J., Birren B.;
RT   "The Genome Sequence of Shigella sp. D9.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-
CC       dephosphocoenzyme-A, the precursor of the prosthetic group of the
CC       holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP
CC       and dephospho-CoA. {ECO:0000256|HAMAP-Rule:MF_00397}.
CC   -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = 2'-(5-triphospho-
CC       alpha-D-ribosyl)-3'-dephospho-CoA + adenine. {ECO:0000256|HAMAP-
CC       Rule:MF_00397, ECO:0000256|SAAS:SAAS00035704}.
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00397}.
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DR   EMBL; GG657387; EGJ07448.1; -; Genomic_DNA.
DR   ProteinModelPortal; F4NLK9; -.
DR   EnsemblBacteria; EGJ07448; EGJ07448; SSJG_03498.
DR   PATRIC; 30982865; VBIShiSp107483_3390.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   HAMAP; MF_00397; CitG; 1.
DR   InterPro; IPR002736; CitG.
DR   InterPro; IPR017551; TriPribosyl-deP-CoA_syn_CitG.
DR   Pfam; PF01874; CitG; 1.
DR   TIGRFAMs; TIGR03125; citrate_citG; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00397,
KW   ECO:0000256|SAAS:SAAS00035693};
KW   Glycosyltransferase {ECO:0000313|EMBL:EGJ07448.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00397,
KW   ECO:0000256|SAAS:SAAS00035701};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00397,
KW   ECO:0000256|SAAS:SAAS00035698}.
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
//