MDCG_PSESM
ID MDCG_PSESM Reviewed; 211 AA.
AC Q87V59;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Phosphoribosyl-dephospho-CoA transferase {ECO:0000255|HAMAP-Rule:MF_00650};
DE EC=2.7.7.66 {ECO:0000255|HAMAP-Rule:MF_00650};
DE AltName: Full=Malonate decarboxylase holo-[acyl-carrier-protein] synthase {ECO:0000255|HAMAP-Rule:MF_00650};
DE Short=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00650};
GN Name=mdcG {ECO:0000255|HAMAP-Rule:MF_00650}; OrderedLocusNames=PSPTO_5082;
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: Transfers 2'-(5-triphosphoribosyl)-3'-dephosphocoenzyme-A to
CC the apo-[acyl-carrier-protein] of the malonate decarboxylase to yield
CC holo-[acyl-carrier-protein]. {ECO:0000255|HAMAP-Rule:MF_00650}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + apo-
CC [malonate decarboxylase ACP] = diphosphate + holo-[malonate
CC decarboxylase ACP]; Xref=Rhea:RHEA:42644, Rhea:RHEA-COMP:10160,
CC Rhea:RHEA-COMP:10161, ChEBI:CHEBI:29999, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61378, ChEBI:CHEBI:82683; EC=2.7.7.66;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00650};
CC -!- SIMILARITY: Belongs to the MdcG family. {ECO:0000255|HAMAP-
CC Rule:MF_00650}.
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DR EMBL; AE016853; AAO58509.1; -; Genomic_DNA.
DR RefSeq; NP_794814.1; NC_004578.1.
DR AlphaFoldDB; Q87V59; -.
DR STRING; 223283.PSPTO_5082; -.
DR EnsemblBacteria; AAO58509; AAO58509; PSPTO_5082.
DR KEGG; pst:PSPTO_5082; -.
DR PATRIC; fig|223283.9.peg.5203; -.
DR eggNOG; ENOG502Z8NU; Bacteria.
DR HOGENOM; CLU_111981_0_0_6; -.
DR OMA; PHDLLWG; -.
DR OrthoDB; 1409077at2; -.
DR PhylomeDB; Q87V59; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00650; Malonate_MdcG; 1.
DR InterPro; IPR017557; Holo-ACP_synthase.
DR Pfam; PF10620; MdcG; 1.
DR TIGRFAMs; TIGR03135; malonate_mdcG; 1.
PE 3: Inferred from homology;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..211
FT /note="Phosphoribosyl-dephospho-CoA transferase"
FT /id="PRO_0000220296"
FT ACT_SITE 136
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
SQ SEQUENCE 211 AA; 22988 MW; A037737A3CD7D04E CRC64;
MIDSAFVVLP HDLLWGMPLS ALPDDAPQWA VDTLLAGQPV VVRRQAMPAG QVAVGLRGRG
REQRYAASMW LTNVYRRVTP EQLIDCPSEH IQDWPALRAL RQVRPVMDAL ERVWGVGGSA
GFELASGIAA LNQDSDLDLI LRTPAPFSRR CAAELVEALA ASVCRVDVQL QLDQGAVALR
EWARPAGRVL LKTASGARLV SDPWHLAEVC A