ID   MDCB_PSEU2              Reviewed;         291 AA.
AC   Q4ZZA9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Psyr_0443;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35513.1; -; Genomic_DNA.
DR   RefSeq; WP_011266406.1; NC_007005.1.
DR   RefSeq; YP_233551.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZZA9; -.
DR   STRING; 205918.Psyr_0443; -.
DR   EnsemblBacteria; AAY35513; AAY35513; Psyr_0443.
DR   KEGG; psb:Psyr_0443; -.
DR   PATRIC; fig|205918.7.peg.460; -.
DR   eggNOG; COG1767; Bacteria.
DR   HOGENOM; CLU_056179_0_0_6; -.
DR   OMA; QSWQRPA; -.
DR   Proteomes; UP000000426; 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..291
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase"
FT                   /id="PRO_0000255405"
SQ   SEQUENCE   291 AA;  30581 MW;  B28D8A623ECE364F CRC64;
     MSALQWSPHP ASLAERLADL AVDALIDEAD LSPKPALVDR RGSGAHTDLH LGLMHSSALS
     LWPTFKWMAD AATQFGVVGQ PLREALGRLG REGEATMLRT TSGVNTHRGA IWALGLLVTA
     AALDAQECAP EAICARAGAL ARIKDRQVLT QNSHGDQVVR RYGVMGAREQ AQQGFPAVRL
     FALPQLQRSR AAGSGEQNAR LDALLAIMTT LDDTCVLHRA GIEGLNAMQQ GAQRVLYAGG
     SVSLAGRRAL NALDQHLLAL NASPGGAADL LAACLFIDGL EPALGPVSRS A