MDCC_BRADU
ID MDCC_BRADU Reviewed; 105 AA.
AC Q89XN9;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=bll0269;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(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}.
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; BA000040; BAC45534.1; -; Genomic_DNA.
DR RefSeq; NP_766909.1; NC_004463.1.
DR RefSeq; WP_011083101.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89XN9; -.
DR SMR; Q89XN9; -.
DR STRING; 224911.27348516; -.
DR EnsemblBacteria; BAC45534; BAC45534; BAC45534.
DR GeneID; 64020130; -.
DR KEGG; bja:bll0269; -.
DR PATRIC; fig|224911.44.peg.8790; -.
DR eggNOG; COG3052; Bacteria.
DR HOGENOM; CLU_173135_0_0_5; -.
DR InParanoid; Q89XN9; -.
DR OMA; KLSFRHT; -.
DR PhylomeDB; Q89XN9; -.
DR Proteomes; UP000002526; 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_0000220283"
FT MOD_RES 28
FT /note="O-(phosphoribosyl dephospho-coenzyme A)serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00710"
SQ SEQUENCE 105 AA; 11207 MW; B15B40CFA9B91CBD CRC64;
MEDLSFRHPV RARADGARRS AIVGIVASGN LEVLVERVLP DAECAIDIKT AAVGFGEVWR
AVIGDFVERY SPGGLKFSIN DGGARPDTVS LRLAQAVRSI AENGQ