ID   MDCC_PSEA8              Reviewed;          99 AA.
AC   B7V2C1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=PLES_02051;
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58;
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA   Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA   Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants of in
RT   vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT   aeruginosa.";
RL   Genome Res. 19:12-23(2009).
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; FM209186; CAW24932.1; -; Genomic_DNA.
DR   RefSeq; WP_012613464.1; NC_011770.1.
DR   AlphaFoldDB; B7V2C1; -.
DR   SMR; B7V2C1; -.
DR   KEGG; pag:PLES_02051; -.
DR   HOGENOM; CLU_173135_1_0_6; -.
DR   OMA; KLSFRHT; -.
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.
FT   CHAIN           1..99
FT                   /note="Malonate decarboxylase acyl carrier protein"
FT                   /id="PRO_1000191173"
FT   MOD_RES         25
FT                   /note="O-(phosphoribosyl dephospho-coenzyme A)serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00710"
SQ   SEQUENCE   99 AA;  10196 MW;  8883E415E6CC5669 CRC64;
     METLTFEFPA GAPARGRALA GCVGSGDLEV LLEPAAGGAL SIQVVTSVNG SGPRWQQLFA
     RVFAAPTAPA ASIRIHDFGA TPGVVRLRLE QALEEAGHD