ID   MDCG_XANAC              Reviewed;         213 AA.
AC   Q8PPW9;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Phosphoribosyl-dephospho-CoA transferase {ECO:0000255|HAMAP-Rule:MF_00650};
DE            EC=2.7.7.66 {ECO:0000255|HAMAP-Rule:MF_00650};
DE   AltName: Full=Malonate decarboxylase holo-[acyl-carrier-protein] synthase {ECO:0000255|HAMAP-Rule:MF_00650};
DE            Short=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00650};
GN   Name=mdcG {ECO:0000255|HAMAP-Rule:MF_00650}; OrderedLocusNames=XAC0564;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Transfers 2'-(5-triphosphoribosyl)-3'-dephosphocoenzyme-A to
CC       the apo-[acyl-carrier-protein] of the malonate decarboxylase to yield
CC       holo-[acyl-carrier-protein]. {ECO:0000255|HAMAP-Rule:MF_00650}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + apo-
CC         [malonate decarboxylase ACP] = diphosphate + holo-[malonate
CC         decarboxylase ACP]; Xref=Rhea:RHEA:42644, Rhea:RHEA-COMP:10160,
CC         Rhea:RHEA-COMP:10161, ChEBI:CHEBI:29999, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61378, ChEBI:CHEBI:82683; EC=2.7.7.66;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00650};
CC   -!- SIMILARITY: Belongs to the MdcG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00650}.
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DR   EMBL; AE008923; AAM35453.1; -; Genomic_DNA.
DR   RefSeq; WP_011050390.1; NC_003919.1.
DR   AlphaFoldDB; Q8PPW9; -.
DR   STRING; 190486.XAC0564; -.
DR   EnsemblBacteria; AAM35453; AAM35453; XAC0564.
DR   GeneID; 66909767; -.
DR   KEGG; xac:XAC0564; -.
DR   eggNOG; ENOG503268I; Bacteria.
DR   HOGENOM; CLU_075747_0_1_6; -.
DR   OMA; GGVNWRE; -.
DR   Proteomes; UP000000576; Chromosome.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00650; Malonate_MdcG; 1.
DR   InterPro; IPR017557; Holo-ACP_synthase.
DR   Pfam; PF10620; MdcG; 1.
DR   TIGRFAMs; TIGR03135; malonate_mdcG; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..213
FT                   /note="Phosphoribosyl-dephospho-CoA transferase"
FT                   /id="PRO_0000220297"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
SQ   SEQUENCE   213 AA;  23013 MW;  C378D8A975C75A17 CRC64;
     MAGRHALVWL REDAQWQAVT SGAQPRLQQW FAAGLPAVVA RGDGSQAPGT LRLGVPLPPS
     EGKQRLALQA HVAGIARCTA PLTLDAVMPH APLAVQPALQ ALLAQAHAHA LHPHVFGSFA
     WQALTGLTYV HAQSDLDLLW SIQTPEQACA VLTLVQRWEQ QHGLRADGEL RLPDDNAVNW
     REYAGNAQQV LVKSNQDCRL LPRAALFPAR SAA