MDCC_XANCP
ID MDCC_XANCP Reviewed; 105 AA.
AC Q8P4U6;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=XCC3610;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
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; AE008922; AAM42880.1; -; Genomic_DNA.
DR RefSeq; NP_638956.1; NC_003902.1.
DR RefSeq; WP_011038694.1; NC_003902.1.
DR AlphaFoldDB; Q8P4U6; -.
DR SMR; Q8P4U6; -.
DR STRING; 340.xcc-b100_0590; -.
DR EnsemblBacteria; AAM42880; AAM42880; XCC3610.
DR KEGG; xcc:XCC3610; -.
DR PATRIC; fig|190485.4.peg.3867; -.
DR eggNOG; COG3052; Bacteria.
DR HOGENOM; CLU_173135_0_0_6; -.
DR OMA; KLSFRHT; -.
DR Proteomes; UP000001010; 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..105
FT /note="Malonate decarboxylase acyl carrier protein"
FT /id="PRO_0000220291"
FT MOD_RES 28
FT /note="O-(phosphoribosyl dephospho-coenzyme A)serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00710"
SQ SEQUENCE 105 AA; 11213 MW; 9F79A3F1718DB5A7 CRC64;
METLRYRFDG RNGARTGLDH ALVGVVASGN LEVLVERVPL GGAMEIEIVT AARGFGEIWQ
AVLDDFAARH SLQDVRISIN DVGATPAVVS LRLEQAIDVL QGADA