ID   CITG_KLEPN              Reviewed;         302 AA.
AC   P45414;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=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;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13882 / NBRC 13541 / NCTC 8172;
RX   PubMed=7830578; DOI=10.1111/j.1365-2958.1994.tb01295.x;
RA   Bott M., Dimroth P.;
RT   "Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase:
RT   localization, sequencing, and expression.";
RL   Mol. Microbiol. 14:347-356(1994).
CC   -!- FUNCTION: Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-
CC       dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-
CC       acyl carrier protein (gamma chain) of citrate lyase, from ATP and
CC       dephospho-CoA. {ECO:0000250}.
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; X79817; CAA56218.1; -; Genomic_DNA.
DR   PIR; S60777; S60777.
DR   RefSeq; WP_004222628.1; NZ_WXZN01000037.1.
DR   AlphaFoldDB; P45414; -.
DR   BRENDA; 2.4.2.52; 2814.
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..302
FT                   /note="2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A
FT                   synthase"
FT                   /id="PRO_0000214669"
SQ   SEQUENCE   302 AA;  32646 MW;  25AAD07DC3580056 CRC64;
     MSDVLINPAR VRRVKPLSAE EVVSAVERAL LTEVRLTPKP GLVDIRNAGA HWDMDLASFE
     ASTAVVAPWM EKFFIMGHDT AAVAPEQVLM MLRPVGMACE NDMLEATGGV NTHRGAIFAF
     GLLSAAAGRL VSKGEPIEQH RLCDQVARFC RGMVMQELSS AGGERLSKGE AHFLRYGLSG
     ARGEAESGFL TVRTQAMPVF TRMMEETGDS NLALLQTLLH LMAWNDDTNL VSRGGLAGLN
     FVQQEAQRLL WQGGVLADGG LEALRQFDDE LIARHLSPGG SADLLAVTWF LSAFPAGALF
     PL