ID   CITG_ALBFT              Reviewed;         302 AA.
AC   Q21VT1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Rfer_2405;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) 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; CP000267; ABD70122.1; -; Genomic_DNA.
DR   RefSeq; WP_011464690.1; NC_007908.1.
DR   AlphaFoldDB; Q21VT1; -.
DR   STRING; 338969.Rfer_2405; -.
DR   EnsemblBacteria; ABD70122; ABD70122; Rfer_2405.
DR   KEGG; rfr:Rfer_2405; -.
DR   eggNOG; COG1767; Bacteria.
DR   HOGENOM; CLU_056179_1_0_4; -.
DR   OMA; MLTPKPG; -.
DR   OrthoDB; 1738403at2; -.
DR   Proteomes; UP000008332; 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_0000255406"
SQ   SEQUENCE   302 AA;  32127 MW;  0EB520558909C378 CRC64;
     MPTATALRID AGSGASDLGE AIGRLAERSL VLELELTPKP GLVDRANSGA HRDMDVGTFR
     ASIAAISPWF SFFFERGVDG SAVPVEDFLR YIRADGMACE RAMFAATLGV NTHKGSVFSF
     GLLCAAAGRL HGRGRPLSRA SVCAEVSHIC AGLVKRELLL PAAARTAGEL LYWQHGLTGA
     RGEAQSGFAT ACAHGVVPYL LARAKGMDEE RSLFEALLQL MAHNRDTNIV SRGGMEGLCL
     VQAEARRLLD CPTPSRSART AQLAAFDQLL IERNLSPGGS ADLLAVSWFL ANLDELVCKC
     VA