ID   MDCG_XANC8              Reviewed;         213 AA.
AC   Q4UZ66;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=XC_0576;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000050; AAY47657.1; -; Genomic_DNA.
DR   RefSeq; WP_011038697.1; NC_007086.1.
DR   AlphaFoldDB; Q4UZ66; -.
DR   EnsemblBacteria; AAY47657; AAY47657; XC_0576.
DR   KEGG; xcb:XC_0576; -.
DR   HOGENOM; CLU_075747_0_1_6; -.
DR   OMA; GGVNWRE; -.
DR   OrthoDB; 1407518at2; -.
DR   Proteomes; UP000000420; 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_1000061475"
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;  22901 MW;  C784E3CD7B061AEF CRC64;
     MAGRHALVWL RADAPSQALT PGAQPRLQAW FAAGFPAVVA RRDGAEQPGQ VRLGVPLPPA
     QGKQRIALCA QVSDIARSVP ALALPEVISH APPQWQAALH ALQAQATAIG MQPRVFGSFA
     FQAVTGLPYV HAASDVDLLW TLDTPTQAHA VVTLLQQWEH VTARRADGEL LLPDGNAVNW
     REYAGDAQQV LVKRNDGCRL LPRTALFPER CAA