ID   CITXG_HAEIN             Reviewed;         465 AA.
AC   P44458;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Protein CitXG;
DE   Includes:
DE     RecName: Full=Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase;
DE              EC=2.7.7.61;
DE     AltName: Full=Apo-ACP nucleodityltransferase;
DE     AltName: Full=Holo-ACP synthase;
DE     AltName: Full=Holo-citrate lyase synthase;
DE   Includes:
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=citXG; Synonyms=citG; OrderedLocusNames=HI_0021;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes formation of 2-(5''-
CC       triphosphoribosyl)-3'-dephosphocoenzyme-A, and then the transfer of
CC       this prosthetic group precursor to the apo-acyl carrier protein (gamma
CC       chain) of the citrate lyase to yield the holo-acyl carrier protein.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + apo-
CC         [citrate lyase ACP] = diphosphate + holo-[citrate lyase ACP];
CC         Xref=Rhea:RHEA:16333, Rhea:RHEA-COMP:10157, Rhea:RHEA-COMP:10158,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:61378,
CC         ChEBI:CHEBI:82683; EC=2.7.7.61;
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: In the N-terminal section; belongs to the CitX family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the CitG/MdcB family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC21699.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L42023; AAC21699.1; ALT_INIT; Genomic_DNA.
DR   PIR; E64140; E64140.
DR   RefSeq; NP_438194.1; NC_000907.1.
DR   AlphaFoldDB; P44458; -.
DR   SMR; P44458; -.
DR   STRING; 71421.HI_0021; -.
DR   EnsemblBacteria; AAC21699; AAC21699; HI_0021.
DR   KEGG; hin:HI_0021; -.
DR   PATRIC; fig|71421.8.peg.21; -.
DR   eggNOG; COG1767; Bacteria.
DR   eggNOG; COG3697; Bacteria.
DR   HOGENOM; CLU_048409_1_0_6; -.
DR   PhylomeDB; P44458; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050519; F:holo-citrate lyase synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   GO; GO:0051191; P:prosthetic group biosynthetic process; IBA:GO_Central.
DR   HAMAP; MF_00397; CitG; 1.
DR   HAMAP; MF_00398; CitX; 1.
DR   InterPro; IPR002736; CitG.
DR   InterPro; IPR005551; CitX.
DR   InterPro; IPR017551; TriPribosyl-deP-CoA_syn_CitG.
DR   PANTHER; PTHR30201; PTHR30201; 1.
DR   Pfam; PF01874; CitG; 1.
DR   Pfam; PF03802; CitX; 1.
DR   TIGRFAMs; TIGR03125; citrate_citG; 1.
DR   TIGRFAMs; TIGR03124; citrate_citX; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..465
FT                   /note="Protein CitXG"
FT                   /id="PRO_0000214682"
FT   REGION          1..182
FT                   /note="Apo-citrate lyase phosphoribosyl-dephospho-CoA
FT                   transferase"
FT   REGION          183..465
FT                   /note="2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A
FT                   synthase"
SQ   SEQUENCE   465 AA;  51835 MW;  4467221C3DB58A96 CRC64;
     MQHFFTTFST EGSKISLEAL LNAREERAIL QQQLITQYGQ TLLCITLTAM GGVKKNALLD
     YVFTKALENL TALFTQLNIT AVKEIIRPLE TGHEAYFVLP IDARTLKVLM IELEESIPLA
     RLWDLDVFNA KGNLLSRTDF DLSPRTCLVC GENAKICART HKHEIDEIVD KIQSLAQNHD
     FAEHIGEQVY LALIQEARLS PKPGLVDAIN NGSHKDMNLH TFEQSAISLK PFFTQFVLKG
     MMTAHLSENQ ILSEIRPLGL LAEKAMFKVT DGVNTHKGAI FSFGLVCTAI GRLLAQKSLV
     QSAVDFDVKL ICSLVAQFTQ GLTDELKNYP EHLPSTAGVR LFQKYGLTGV RGEAENGFNL
     IQTLLPQFDE YHQLEWEHRL LILLLNLMAI NSDTNVVHRG GLAGLYFIQQ TAQDLLTDQH
     LVTDKTALTQ ALMKFDTACI ERNLSSGGSA DLLALTIFFL SFRGN