ID   MDCB_MALRU              Reviewed;         316 AA.
AC   O06922;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Probable 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; Synonyms=madG;
OS   Malonomonas rubra.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Malonomonas.
OX   NCBI_TaxID=57040;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9128730; DOI=10.1111/j.1432-1033.1997.00103.x;
RA   Berg M., Hilbi H., Dimroth P.;
RT   "Sequence of a gene cluster from Malonomonas rubra encoding components of
RT   the malonate decarboxylase Na+ pump and evidence for their function.";
RL   Eur. J. Biochem. 245:103-115(1997).
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.
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   ---------------------------------------------------------------------------
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; U87980; AAC45398.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06922; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   InterPro; IPR002736; CitG.
DR   PANTHER; PTHR30201; PTHR30201; 1.
DR   Pfam; PF01874; CitG; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Transferase.
FT   CHAIN           1..316
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase"
FT                   /id="PRO_0000214672"
SQ   SEQUENCE   316 AA;  34254 MW;  9CB58467DDDB5D60 CRC64;
     MVARGNVVSI GQIAPKHSSE VSFSVDPVSW EIGSLLQRGM LLEVATSNKP GLVCPQSNGC
     HEDMSLMTFM VSSSVIFPAL VMCTQAGRDH EGDLPLLLPV VRGIGAPYEK ELFAATKGVN
     TQKGALFSAA ILAGAAGYLS QKSRHFQIGE LFEVVAAMTK GIVRRELNPS VLEKKESLSN
     GEKLYLRHQV PGIRGELERG LPSVRDYAVP ALKYAQDLGA SLEASFLHTL ITLMSQVDDT
     NIISRGGLES LKKVKTLSKE VLKEGSIFNK EGIDNYFYLE NFCIDRGLSP GGSADLLAIT
     ISAYLLSEEK FKCKIM