ID   CITG_CITK8              Reviewed;         302 AA.
AC   A8AJJ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=CKO_02546;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV13655.1; -; Genomic_DNA.
DR   RefSeq; WP_012133374.1; NC_009792.1.
DR   AlphaFoldDB; A8AJJ2; -.
DR   STRING; 290338.CKO_02546; -.
DR   EnsemblBacteria; ABV13655; ABV13655; CKO_02546.
DR   GeneID; 45136420; -.
DR   KEGG; cko:CKO_02546; -.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; MLTPKPG; -.
DR   OrthoDB; 1738403at2; -.
DR   Proteomes; UP000008148; 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..302
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase"
FT                   /id="PRO_1000049594"
SQ   SEQUENCE   302 AA;  32831 MW;  122498F9338987BD CRC64;
     MMPIPATSTD SAAIPQTLLD AYALLAWRAM LTEVNLSPKP GLVDRINCGA HKDMALEDFH
     RSALAIQGWL PRFIEYGASC AQLPSDDVLK GLRPLGMACE ADMFRATAGV NTHKGSIFSL
     GLLCAAIGRL HQQHSPITPA NICSTAATFC RGLTERELRQ NNQQLTAGQR LYQQLGLTGA
     RGEAEAGYPL VIRHALPHYR ALLAQGRDPE LALLDTLLLL ISMNGDTNVA SRGGAEGLCW
     IQQQATTLLR QGGIRSPADL EHLHRFDQQC IARNLSPGGS ADLLIVTWFL AQISQVNHLH
     NY