ID   MDCG_XANC5              Reviewed;         213 AA.
AC   Q3BY34;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=XCV0598;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ22229.1; -; Genomic_DNA.
DR   RefSeq; WP_011346232.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BY34; -.
DR   SMR; Q3BY34; -.
DR   STRING; 456327.BJD11_19830; -.
DR   EnsemblBacteria; CAJ22229; CAJ22229; XCV0598.
DR   KEGG; xcv:XCV0598; -.
DR   eggNOG; ENOG503268I; Bacteria.
DR   HOGENOM; CLU_075747_0_1_6; -.
DR   OMA; GGVNWRE; -.
DR   Proteomes; UP000007069; 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_1000061474"
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;  23173 MW;  044B4B742A655939 CRC64;
     MAGRHALVWL REDAQWQAVT PGAQPRLRQW FAAGLPAVVA RGDGSQAPGS VRLGVPLPPS
     EGKQRLALQA HVADIARCTA PLTLDAVTPQ APVAVQPLLQ ALLAQARAHA LRPHVFGSFA
     WQALTGLTYV HAQSDLDLLW PIETPEQARA LVTLLQRWEQ QHGLRADGEL LLPEDNAVNW
     REYAGTAQQV LVKSNQDCRL LPRAALFPVR SAA