ID   MDCG_KLEPN              Reviewed;         205 AA.
AC   P71426; O32716;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Phosphoribosyl-dephospho-CoA transferase;
DE            EC=2.7.7.66;
DE   AltName: Full=Malonate decarboxylase holo-[acyl-carrier-protein] synthase;
DE            Short=Holo-ACP synthase;
GN   Name=mdcG; Synonyms=mdcF;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9208947; DOI=10.1111/j.1432-1033.1997.00530.x;
RA   Hoenke S., Schmid M., Dimroth P.;
RT   "Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate
RT   decarboxylase and expression of the enzyme in Escherichia coli.";
RL   Eur. J. Biochem. 246:530-538(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CG43;
RA   Chang H., Deng W., Chaou S., Lee R., Peng H.;
RT   "Molecular characterization of the malonate utilization system in
RT   Klebsiella pneumoniae.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11052675; DOI=10.1021/bi0011532;
RA   Hoenke S., Wild M.R., Dimroth P.;
RT   "Biosynthesis of triphosphoribosyl-dephospho-coenzyme A, the precursor of
RT   the prosthetic group of malonate decarboxylase.";
RL   Biochemistry 39:13223-13232(2000).
RN   [4]
RP   ACTIVE SITES, AND MUTAGENESIS OF ASP-134 AND ASP-136.
RX   PubMed=11052676; DOI=10.1021/bi001154u;
RA   Hoenke S., Schmid M., Dimroth P.;
RT   "Identification of the active site of phosphoribosyl-dephospho-coenzyme A
RT   transferase and relationship of the enzyme to an ancient class of
RT   nucleotidyltransferases.";
RL   Biochemistry 39:13233-13240(2000).
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:0000269|PubMed:11052675}.
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:0000269|PubMed:11052675};
CC   -!- SIMILARITY: Belongs to the MdcG family. {ECO:0000305}.
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DR   EMBL; U95087; AAC45459.1; -; Genomic_DNA.
DR   EMBL; U56096; AAA99821.1; -; Genomic_DNA.
DR   RefSeq; WP_004152239.1; NZ_WYAL01000007.1.
DR   RefSeq; WP_004209784.1; NZ_WXZO01000032.1.
DR   AlphaFoldDB; P71426; -.
DR   OrthoDB; 1409077at2; -.
DR   BioCyc; MetaCyc:MON-14204; -.
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   1: Evidence at protein level;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..205
FT                   /note="Phosphoribosyl-dephospho-CoA transferase"
FT                   /id="PRO_0000220293"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000269|PubMed:11052676"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000269|PubMed:11052676"
FT   MUTAGEN         134
FT                   /note="D->A: Abolishes transfer of prosthetic group to acyl
FT                   carrier protein."
FT                   /evidence="ECO:0000269|PubMed:11052676"
FT   MUTAGEN         136
FT                   /note="D->A: Abolishes transfer of prosthetic group to acyl
FT                   carrier protein."
FT                   /evidence="ECO:0000269|PubMed:11052676"
FT   CONFLICT        30
FT                   /note="Q -> H (in Ref. 2; AAA99821)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   205 AA;  23014 MW;  1EFB8FE1053F06E4 CRC64;
     MSATPRPHDL VWLNHASALE DIAEPWVAQQ WRAALPVVVR RDVDDQARVP VGVRGMKREQ
     RAAGWVQARN IVRSVTPEML VDREVLLHSP FVSQPPVQGA IALTLHRWPW GWGVTGSTGY
     ALATEIPVLH AASDLDLLIR APQPLDREAL LEWQTRVAQL PCRADTQVET PYGAFALNEW
     LRDGRALLKT SRGARLTATP WHREE