ID   MDCG_PSEPW              Reviewed;         204 AA.
AC   B1J9E4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
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};
GN   OrderedLocusNames=PputW619_2878;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000949; ACA73370.1; -; Genomic_DNA.
DR   RefSeq; WP_012314728.1; NC_010501.1.
DR   AlphaFoldDB; B1J9E4; -.
DR   STRING; 390235.PputW619_2878; -.
DR   EnsemblBacteria; ACA73370; ACA73370; PputW619_2878.
DR   KEGG; ppw:PputW619_2878; -.
DR   eggNOG; ENOG502Z8NU; Bacteria.
DR   HOGENOM; CLU_111981_0_0_6; -.
DR   OMA; PHDLLWG; -.
DR   OrthoDB; 1409077at2; -.
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..204
FT                   /note="Phosphoribosyl-dephospho-CoA transferase"
FT                   /id="PRO_1000130987"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
SQ   SEQUENCE   204 AA;  21471 MW;  D7A221BEC55C2D8B CRC64;
     MSAPQPHDLL WGMTPAALPV DAPAWATQVL AAGQPVVVRR ACCAAGWVAV GLRGEGRAQR
     LGVQMRLADI RRQLRPEALR GQGTSPWAAL QALASVAPVL DACGLAWGPT GGVGYQLATG
     VEVLHAASDL DLLLRTPRPM SRAKARELLD SLDCSPCRID VQLQTPAGGI ALREWAGVAQ
     RVLLKSALGA RLVADPWNLL ECAA