ID   MDCB_KLEPN              Reviewed;         280 AA.
AC   P71422;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase;
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase;
DE            EC=2.4.2.52;
GN   Name=mdcB;
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.
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).
CC   -!- FUNCTION: Involved in the formation of 2-(5''-phosphoribosyl)-3'-
CC       dephosphocoenzyme-A, the prosthetic group of the acyl-carrier protein
CC       of the malonate decarboxylase. {ECO:0000269|PubMed:11052675}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-
CC         3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57328, ChEBI:CHEBI:61378; EC=2.4.2.52;
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA99817.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U95087; AAC45454.1; -; Genomic_DNA.
DR   EMBL; U56096; AAA99817.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; WP_004143107.1; NZ_WYAM01000003.1.
DR   AlphaFoldDB; P71422; -.
DR   OrthoDB; 1738403at2; -.
DR   BioCyc; MetaCyc:MON-14203; -.
DR   BRENDA; 2.4.2.52; 2814.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   HAMAP; MF_01883; MdcB; 1.
DR   InterPro; IPR002736; CitG.
DR   InterPro; IPR017555; TriPribosyl-deP-CoA_syn.
DR   PANTHER; PTHR30201; PTHR30201; 1.
DR   Pfam; PF01874; CitG; 1.
DR   TIGRFAMs; TIGR03132; malonate_mdcB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Transferase.
FT   CHAIN           1..280
FT                   /note="2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A
FT                   synthase"
FT                   /id="PRO_0000214671"
SQ   SEQUENCE   280 AA;  29213 MW;  AA2E7979B2E7B5A3 CRC64;
     MKNLSPLHAE SRVSWLAHTA SACLIDEARL SPKPGLVDSR GNGAHQDLNL ALMERSARSL
     QPTFHALAEQ SWRRPADIAL RETVGRLGRE GEAQMMLATG GVNTHRGAIW ALGLLVSAVA
     MLGGEGQSQA IADAAAALAR LPDGFAPKSF SKGLRASRRW QVPGAREEAQ CGFPHITRLA
     LPQLQHSRAR GASEPQAQLD ALMAIMTSLS DTCVLSRAGM AGLQAMQQGA CEVLAAGGCA
     SFAGRAALAR LDAIMLALNA SPGGAADLLA ATLFLDRVAG