ID   CITG_HAEDU              Reviewed;         323 AA.
AC   O30827;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 114.
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; OrderedLocusNames=HD_1245;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RX   PubMed=9511768; DOI=10.1016/s0378-1119(97)00642-2;
RA   San Mateo L.R., Toffer K.L., Kawula T.H.;
RT   "The sodA gene of Haemophilus ducreyi encodes a hydrogen peroxide-
RT   inhibitable superoxide dismutase.";
RL   Gene 207:251-257(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: This protein seems to consist of a CitG domain with an
CC       incomplete N-terminal CitX region. The start site is approximate as
CC       there is similarity downstream up to the C-terminal codon of the
CC       adjacent sodA gene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP96080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF017750; AAC46220.1; -; Genomic_DNA.
DR   EMBL; AE017143; AAP96080.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; O30827; -.
DR   SMR; O30827; -.
DR   STRING; 233412.HD_1245; -.
DR   EnsemblBacteria; AAP96080; AAP96080; HD_1245.
DR   KEGG; hdu:HD_1245; -.
DR   eggNOG; COG1767; Bacteria.
DR   eggNOG; COG3697; Bacteria.
DR   HOGENOM; CLU_048409_1_0_6; -.
DR   Proteomes; UP000001022; 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..323
FT                   /note="2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A
FT                   synthase"
FT                   /id="PRO_0000214668"
SQ   SEQUENCE   323 AA;  35978 MW;  E39389C4AF1BC8E1 CRC64;
     MCAESAKICA RSRRHSIDDL LSEIHTRAQQ YYFSEQIAEL AYQALIKEAR LTPKPGLVDS
     TNNGSHQDMS LSTFEQSAIA LRPFFTQFVL MGIETTNLPD SHILSKIRPL GLQAEQAMFV
     ATNQVNTHKG AIFAFGLVCT ALGRHFSRWQ NKMMSSPSFE ISQDTTGISL ISETVARFTQ
     GITDELKNYS KNQPLTAGIT LYQQYGFTGA RGEAEKGFPL VQQAVVFILS QAESEMRWYW
     ALLYLMANNN DTNIVHRGGI NGLQFIQDEA HKRLGNAKNL QNANALMASL REFDDDCIAR
     NLSPGGSADL LALTIFFLSL LYC