ID   MDCC_XANAC              Reviewed;         105 AA.
AC   Q8PPX2;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=XAC0561;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008923; AAM35450.1; -; Genomic_DNA.
DR   RefSeq; WP_005914105.1; NC_003919.1.
DR   AlphaFoldDB; Q8PPX2; -.
DR   SMR; Q8PPX2; -.
DR   STRING; 190486.XAC0561; -.
DR   EnsemblBacteria; AAM35450; AAM35450; XAC0561.
DR   GeneID; 66909764; -.
DR   KEGG; xac:XAC0561; -.
DR   eggNOG; COG3052; Bacteria.
DR   HOGENOM; CLU_173135_0_0_6; -.
DR   OMA; KLSFRHT; -.
DR   Proteomes; UP000000576; 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.
FT   CHAIN           1..105
FT                   /note="Malonate decarboxylase acyl carrier protein"
FT                   /id="PRO_0000220290"
FT   MOD_RES         28
FT                   /note="O-(phosphoribosyl dephospho-coenzyme A)serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00710"
SQ   SEQUENCE   105 AA;  11263 MW;  D15AA8E618B47E16 CRC64;
     METLRYRFDG QRGARAGLEH ALVGVVASGN LEVLVERVPL EGAMEIDILT AARGFGAIWQ
     AVLDDFAARH PLRDVRISIN DVGATPAVVS LRLEQALDVL QGADA