MDCB_PSESM
ID MDCB_PSESM Reviewed; 291 AA.
AC Q87V55;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=PSPTO_5086;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO58513.1; -; Genomic_DNA.
DR RefSeq; NP_794818.1; NC_004578.1.
DR RefSeq; WP_011105305.1; NC_004578.1.
DR AlphaFoldDB; Q87V55; -.
DR STRING; 223283.PSPTO_5086; -.
DR EnsemblBacteria; AAO58513; AAO58513; PSPTO_5086.
DR GeneID; 1186771; -.
DR KEGG; pst:PSPTO_5086; -.
DR PATRIC; fig|223283.9.peg.5207; -.
DR eggNOG; COG1767; Bacteria.
DR HOGENOM; CLU_056179_0_0_6; -.
DR OMA; QSWQRPA; -.
DR OrthoDB; 1738403at2; -.
DR PhylomeDB; Q87V55; -.
DR Proteomes; UP000002515; 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..291
FT /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT dephosphocoenzyme-A synthase"
FT /id="PRO_1000189591"
SQ SEQUENCE 291 AA; 30381 MW; C8A106DDE8CFA48A CRC64;
MSALQRTPQP ASLAERLADL AVDALIDEAD LSPKPALVDR CSNGAHTDLH LGLMHSSALS
LWPTFKLMAD AAAQFQAVGE PLREALGRLG REGEATMLRT TSGVNTHRGA IWALGLLVTA
AALDPQDCGP DAVCQRAASL ALIKDRQVLA QNSHGSEVVR RYGVMGAREQ AQHGFPAVIR
CALPQLQRSR AAGSGEQNAR LDALLAIMTT LADTCVLHRA GLEGLQTMQN GAQRVLDAGG
SASLAGRRAL NQLDQQLLAL NASPGGAADL LAACLFIDGL EPALGPVSRS A
