ID   MDCB_PSEU5              Reviewed;         290 AA.
AC   A4VRZ0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=PST_4119;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP81741.1; -; Genomic_DNA.
DR   RefSeq; WP_011915120.1; NC_009434.1.
DR   AlphaFoldDB; A4VRZ0; -.
DR   STRING; 379731.PST_4119; -.
DR   EnsemblBacteria; ABP81741; ABP81741; PST_4119.
DR   KEGG; psa:PST_4119; -.
DR   eggNOG; COG1767; Bacteria.
DR   HOGENOM; CLU_056179_0_0_6; -.
DR   OMA; QSWQRPA; -.
DR   Proteomes; UP000000233; 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; Reference proteome; Transferase.
FT   CHAIN           1..290
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase"
FT                   /id="PRO_1000189589"
SQ   SEQUENCE   290 AA;  29727 MW;  9B12D01DA4F06A84 CRC64;
     MSALIARQAP SAAERLADLA VQALVDEADL SPKPGLVDRR GSGAHSDLHL GLMHASAQSL
     WPAFAAMADA ARSEGRVSQA LRETLGQLGR DGEAEMLRVT AGVNTHRGAI WALGLLSAAA
     MLESGASAGG IAASAAALAR LDDPAAPHNP DSHGARVCRR YGVLGAREQA QHGFPAVIEH
     GLPQLLASRR AGAGEQNARL DALLAIMSSL TDTCVLHRAG LEGLTRMQAG ARAVLEAGGC
     ASLAGRRRLR ALEGEMLSLR ASPGGAADLL AATLFLDRLT PAASAPIGSY