(data stored in SCRATCH zone)

SWISSPROT: C8U2X6_ECO10

ID   C8U2X6_ECO10            Unreviewed;       292 AA.
AC   C8U2X6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
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:BAI29484.1};
GN   OrderedLocusNames=ECO103_0621 {ECO:0000313|EMBL:BAI29484.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29484.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29484.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00397, ECO:0000256|SAAS:SAAS01125469};
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00397}.
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DR   EMBL; AP010958; BAI29484.1; -; Genomic_DNA.
DR   RefSeq; WP_000062457.1; NC_013353.1.
DR   EnsemblBacteria; BAI29484; BAI29484; ECO103_0621.
DR   KEGG; eoh:ECO103_0621; -.
DR   HOGENOM; HOG000258582; -.
DR   KO; K05966; -.
DR   OMA; QSWQRPA; -.
DR   BioCyc; ECOL585395:ECO103_RS03240-MONOMER; -.
DR   Proteomes; UP000000959; 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; C8U2X6.
DR   SWISS-2DPAGE; C8U2X6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00397,
KW   ECO:0000256|SAAS:SAAS01057247};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00397,
KW   ECO:0000256|SAAS:SAAS01057252};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00397,
KW   ECO:0000256|SAAS:SAAS01057253, ECO:0000313|EMBL:BAI29484.1}.
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
//

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