ID   MDCC_STRMK              Reviewed;         106 AA.
AC   B2FSQ5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=Smlt1231;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(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}.
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DR   EMBL; AM743169; CAQ44787.1; -; Genomic_DNA.
DR   RefSeq; WP_005408516.1; NC_010943.1.
DR   AlphaFoldDB; B2FSQ5; -.
DR   SMR; B2FSQ5; -.
DR   STRING; 522373.Smlt1231; -.
DR   EnsemblBacteria; CAQ44787; CAQ44787; Smlt1231.
DR   KEGG; sml:Smlt1231; -.
DR   eggNOG; COG3052; Bacteria.
DR   HOGENOM; CLU_173135_0_0_6; -.
DR   OMA; KLSFRHT; -.
DR   OrthoDB; 1955361at2; -.
DR   Proteomes; UP000008840; 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..106
FT                   /note="Malonate decarboxylase acyl carrier protein"
FT                   /id="PRO_1000191175"
FT   MOD_RES         28
FT                   /note="O-(phosphoribosyl dephospho-coenzyme A)serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00710"
SQ   SEQUENCE   106 AA;  11311 MW;  01D2A32A41D33317 CRC64;
     METLDYRFEG HTAVQFPRGA VLVGVLASGN LEILLEPAAL DGAMTVRIIT AAKGFGSVWQ
     AVISDFAQRH PLRDVRISIN DAGATPAVVS LRLDQAVETL LAGEPR