ID   MDCC_PSEU5              Reviewed;          99 AA.
AC   A4VRY9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Malonate decarboxylase acyl carrier protein {ECO:0000255|HAMAP-Rule:MF_00710};
DE   AltName: Full=Malonate decarboxylase subunit delta {ECO:0000255|HAMAP-Rule:MF_00710};
GN   Name=mdcC {ECO:0000255|HAMAP-Rule:MF_00710}; OrderedLocusNames=PST_4118;
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: Subunit of malonate decarboxylase, it is an acyl carrier
CC       protein to which acetyl and malonyl thioester residues are bound via a
CC       2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over
CC       during the catalytic mechanism. {ECO:0000255|HAMAP-Rule:MF_00710}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00710}.
CC   -!- PTM: Covalently binds the prosthetic group of malonate decarboxylase.
CC       {ECO:0000255|HAMAP-Rule:MF_00710}.
CC   -!- SIMILARITY: Belongs to the MdcC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00710}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000304; ABP81740.1; -; Genomic_DNA.
DR   RefSeq; WP_003296879.1; NC_009434.1.
DR   AlphaFoldDB; A4VRY9; -.
DR   SMR; A4VRY9; -.
DR   STRING; 379731.PST_4118; -.
DR   EnsemblBacteria; ABP81740; ABP81740; PST_4118.
DR   KEGG; psa:PST_4118; -.
DR   eggNOG; COG3052; Bacteria.
DR   HOGENOM; CLU_173135_1_0_6; -.
DR   OMA; KLSFRHT; -.
DR   Proteomes; UP000000233; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00710; Malonate_deCO2ase_dsu; 1.
DR   InterPro; IPR023439; Mal_deCO2ase/Cit_lyase_ACP.
DR   InterPro; IPR009662; Malonate_deCO2ase_dsu.
DR   Pfam; PF06857; ACP; 1.
DR   TIGRFAMs; TIGR03130; malonate_delta; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..99
FT                   /note="Malonate decarboxylase acyl carrier protein"
FT                   /id="PRO_0000303112"
FT   MOD_RES         25
FT                   /note="O-(phosphoribosyl dephospho-coenzyme A)serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00710"
SQ   SEQUENCE   99 AA;  10726 MW;  CF47D722078BE84A CRC64;
     METLSFEFAA GQPARGKALV GVVGSGDLEV LLEPGQAGKL AIQVVTSVNG AEQRWQQLFE
     RMFREQTPPA LNIDIHDFGA TPGVVRLRLE QGLEEVGHD