ID   MDCB_PSEAB              Reviewed;         293 AA.
AC   Q02UM6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=PA14_02560;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ15158.1; -; Genomic_DNA.
DR   RefSeq; WP_003137092.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02UM6; -.
DR   PRIDE; Q02UM6; -.
DR   EnsemblBacteria; ABJ15158; ABJ15158; PA14_02560.
DR   KEGG; pau:PA14_02560; -.
DR   HOGENOM; CLU_056179_0_0_6; -.
DR   OMA; QSWQRPA; -.
DR   BioCyc; PAER208963:G1G74-211-MON; -.
DR   Proteomes; UP000000653; 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_1000049597"
SQ   SEQUENCE   293 AA;  30603 MW;  F149D3ABD06077DF CRC64;
     MNAIANLAAT LRADLGECLA DLAVDALIDE AELSPKPALV DRRGNGAHAD LHLGLMQASA
     LSLWPCFKEM ADAAQRHGRI DARLRGVLGQ LGRDGEAAML RTTEGVNTHR GAIWALGLLV
     AAAALEPRRT QAGEVAARAG RIALLDDPAA AIGDSHGERV RRRYGVGGAR EEARLGFPRA
     VRHGLPQLWR SREGGAGEQN ARLDALLAIM SVLDDTCVLH RAGRVGLAAM QDGARAVLAA
     GGSASLAGRR RLCELDRRLL ALNASPGGAA DLLAACLFLD RLPAVSGGWA GSL