CITG_STRP1
ID CITG_STRP1 Reviewed; 294 AA.
AC P58159; Q48YQ6;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase;
DE Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase;
DE EC=2.4.2.52;
GN Name=citG; OrderedLocusNames=SPy_1178, M5005_Spy0898;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
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 -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000305}.
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DR EMBL; AE004092; AAK34045.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51516.1; -; Genomic_DNA.
DR RefSeq; NP_269324.1; NC_002737.2.
DR AlphaFoldDB; P58159; -.
DR PaxDb; P58159; -.
DR EnsemblBacteria; AAK34045; AAK34045; SPy_1178.
DR KEGG; spy:SPy_1178; -.
DR KEGG; spz:M5005_Spy0898; -.
DR PATRIC; fig|160490.10.peg.1029; -.
DR HOGENOM; CLU_056179_1_0_9; -.
DR OMA; QSWQRPA; -.
DR Proteomes; UP000000750; 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; Reference proteome; Transferase.
FT CHAIN 1..294
FT /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT dephosphocoenzyme-A synthase"
FT /id="PRO_0000214677"
SQ SEQUENCE 294 AA; 32770 MW; 84F51F444FA53844 CRC64;
MTKAVLTSIS QLALKALLYE VSLSPKPGLV DRFDNGAHDD MSFITFIDSM IALSPFFQAY
IETGFAYAKE EPLLLFNRLR QLGQKAEETM FCATQGINTH KGLNFSMALL LGATGAYLAR
TPHLMTDLGR FSKEDTLAIC RLVKPMTAHL IQTDLGHLNT KKEFTYGEQL FVTYGIKGPR
GEASEGFTTL TDHALPYFRQ MISQNDPETS QLRLLVYLMS IVEDGNLIHR GGIEAWKGVK
ADMRLLLQQD LSTTDLRLAL SSYNQCLINQ HLSPGGAADL LALTFYFAFL EKLL