ID   MDCB_PSEA7              Reviewed;         293 AA.
AC   A6UY04;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase {ECO:0000255|HAMAP-Rule:MF_01883};
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase {ECO:0000255|HAMAP-Rule:MF_01883};
DE            EC=2.4.2.52 {ECO:0000255|HAMAP-Rule:MF_01883};
GN   Name=mdcB {ECO:0000255|HAMAP-Rule:MF_01883}; OrderedLocusNames=PSPA7_0293;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01883}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01883};
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01883}.
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DR   EMBL; CP000744; ABR85098.1; -; Genomic_DNA.
DR   RefSeq; WP_012073851.1; NC_009656.1.
DR   AlphaFoldDB; A6UY04; -.
DR   EnsemblBacteria; ABR85098; ABR85098; PSPA7_0293.
DR   KEGG; pap:PSPA7_0293; -.
DR   HOGENOM; CLU_056179_0_0_6; -.
DR   OMA; QSWQRPA; -.
DR   OrthoDB; 1738403at2; -.
DR   Proteomes; UP000001582; Chromosome.
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..293
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase"
FT                   /id="PRO_1000049596"
SQ   SEQUENCE   293 AA;  30640 MW;  A8E5DE56F023C14D CRC64;
     MNAIANLAAT PRADLGECLA DLAVDALIDE AELSPKPALV DRRGNGAHAD LHLGLMQASA
     LSLWPCFKEM ADAAQRHARI DARLRGVLGQ LGREGEVAML RTTEGVNSHR GAIWALGLLV
     AAAALAPRRT QAGEVAARAG RIALLDDPAA ASGDSHGERV RRRYGVGGAR EEARLGFPRA
     VRHGLPQLWR SRESGAGEQN ARLDALLAIM SVLDDTCVLH RAGRVGLAAM QEGARAVLAA
     GGSASLAGRR RLRELDRRLL ALNASPGGAA DLLAACLFLD RLPAALGGWA GSL