ID   MDCG_PSEF5              Reviewed;         208 AA.
AC   Q4K4G0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=PFL_5815;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(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; CP000076; AAY95005.1; -; Genomic_DNA.
DR   RefSeq; WP_011063989.1; NC_004129.6.
DR   AlphaFoldDB; Q4K4G0; -.
DR   STRING; 220664.PFL_5815; -.
DR   EnsemblBacteria; AAY95005; AAY95005; PFL_5815.
DR   KEGG; pfl:PFL_5815; -.
DR   PATRIC; fig|220664.5.peg.5929; -.
DR   eggNOG; ENOG502Z8NU; Bacteria.
DR   HOGENOM; CLU_111981_0_0_6; -.
DR   OMA; PHDLLWG; -.
DR   OrthoDB; 1409077at2; -.
DR   Proteomes; UP000008540; 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; Reference proteome; Transferase.
FT   CHAIN           1..208
FT                   /note="Phosphoribosyl-dephospho-CoA transferase"
FT                   /id="PRO_1000061472"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
SQ   SEQUENCE   208 AA;  22229 MW;  A51F239C5442523D CRC64;
     MSGCGPWLPH DLLWGMTPAQ LPGDAPAWAH AVLEAGQPVV VRRALTAPGQ VAVGLRGVSR
     EQRYPALLDL QAVQRGVRPE QLCHVPPQGP WPALQALQHL RDELDAQEWI WGVSGSAGFE
     LASGVAALHQ HSDLDLILRT PELLPRARAR ELLALLDGAG CPVDMQLQVP GGALALREWA
     GPAARVLLKS ASGARLVSDP WNPQEQAA