ID   CITG_STRP6              Reviewed;         294 AA.
AC   Q5XC41;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Probable 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}; OrderedLocusNames=M6_Spy0887;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
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:0000255|HAMAP-Rule:MF_00397};
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00397}.
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DR   EMBL; CP000003; AAT87022.1; -; Genomic_DNA.
DR   RefSeq; WP_011184522.1; NC_006086.1.
DR   AlphaFoldDB; Q5XC41; -.
DR   PRIDE; Q5XC41; -.
DR   EnsemblBacteria; AAT87022; AAT87022; M6_Spy0887.
DR   KEGG; spa:M6_Spy0887; -.
DR   HOGENOM; CLU_056179_1_0_9; -.
DR   OMA; QSWQRPA; -.
DR   Proteomes; UP000001167; 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;
KW   ATP-binding; Nucleotide-binding; Transferase.
FT   CHAIN           1..294
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase"
FT                   /id="PRO_0000214679"
SQ   SEQUENCE   294 AA;  32717 MW;  F625D92970D15DDD CRC64;
     MTKAVLTSIS QLALKALLYE VSLSPKPGLV DRFDNGAHDD MSFMTFIDSM IALSPFFQAY
     IETGFAYAKE EPLLLFNRLR QLGQKAEEIM FCATQGINTH KGLNFSMALL LGATGAYLAR
     TPHLMTDLGC FSKEDTLAIC RLVKPMTAHL IQADLGHLNT KKEFTYGEQL FVTYGIKGPR
     GEASEGFTTL TDHALPYFRQ MISQNDPETS QLRLLVYLMS IVEDGNLIHR GGIEAWKGVK
     ADMRLLLQQD LSTTDLRLAL SSYNQCLINQ HLSPGGAADL LALTFYFAFL EKLL