(data stored in ACNUC7421 zone)

SWISSPROT: CITG_ECO27

ID   CITG_ECO27              Reviewed;         292 AA.
AC   B7UKQ5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase {ECO:0000255|HAMAP-Rule:MF_00397};
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase {ECO:0000255|HAMAP-Rule:MF_00397};
DE            EC=2.4.2.52 {ECO:0000255|HAMAP-Rule:MF_00397};
GN   Name=citG {ECO:0000255|HAMAP-Rule:MF_00397};
GN   OrderedLocusNames=E2348C_0514;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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:0000255|HAMAP-Rule:MF_00397}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-
CC         ribosyl)-3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117,
CC         ChEBI:CHEBI:16708, ChEBI:CHEBI:30616, ChEBI:CHEBI:57328,
CC         ChEBI:CHEBI:61378; EC=2.4.2.52; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00397};
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00397}.
DR   EMBL; FM180568; CAS08062.1; -; Genomic_DNA.
DR   RefSeq; WP_000062476.1; NC_011601.1.
DR   EnsemblBacteria; CAS08062; CAS08062; E2348C_0514.
DR   KEGG; ecg:E2348C_0514; -.
DR   KO; K05966; -.
DR   OMA; QSWQRPA; -.
DR   BioCyc; ECOL574521:E2348C_RS02700-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR30201; PTHR30201; 1.
DR   Pfam; PF01874; CitG; 1.
DR   TIGRFAMs; TIGR03125; citrate_citG; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKQ5.
DR   SWISS-2DPAGE; B7UKQ5.
KW   ATP-binding; Complete proteome; Nucleotide-binding; Transferase.
FT   CHAIN         1    292       2-(5''-triphosphoribosyl)-3'-
FT                                dephosphocoenzyme-A synthase.
FT                                /FTId=PRO_1000189586.
SQ   SEQUENCE   292 AA;  31637 MW;  6465CAB851835AF3 CRC64;
     MSMPATSTKT TKLATSLIDE YALLGWRAML TEVNLSPKPG LVDRINCGAH KDMALEDFHR
     SALAIQGWLP RFIEFGACSA EMAPEAVLNG LRPIGMACEG DMFRATAGVN THKGSIFSLG
     LLCAAIGRLL QLNQPVTPTT VCSTAASFCR GLTDRELRTN NSRLTAGQRL YQQLGLTGAR
     GEAEAGYPLV INHALPHYLT LLDQGLDPEL ALLDTLLLLM ATNGDTNVAS RGGEGGLRWL
     QREAQTLLQK GGIRTPADLD YLRQFDRECI ERNLSPGGSA DLLILTWFLA QI
//

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