MDCC_PSEPG
ID MDCC_PSEPG Reviewed; 99 AA.
AC B0KQS4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
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};
GN OrderedLocusNames=PputGB1_2440;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000926; ABY98339.1; -; Genomic_DNA.
DR RefSeq; WP_012272082.1; NC_010322.1.
DR AlphaFoldDB; B0KQS4; -.
DR SMR; B0KQS4; -.
DR STRING; 76869.PputGB1_2440; -.
DR EnsemblBacteria; ABY98339; ABY98339; PputGB1_2440.
DR KEGG; ppg:PputGB1_2440; -.
DR eggNOG; COG3052; Bacteria.
DR HOGENOM; CLU_173135_1_0_6; -.
DR OMA; KLSFRHT; -.
DR Proteomes; UP000002157; 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..99
FT /note="Malonate decarboxylase acyl carrier protein"
FT /id="PRO_1000083202"
FT MOD_RES 25
FT /note="O-(phosphoribosyl dephospho-coenzyme A)serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00710"
SQ SEQUENCE 99 AA; 10694 MW; B023428FE6CC1545 CRC64;
METLTFNFPA AEPGRGRTLV GCVSSGDLEV LIEPGTAGSL QIQVVTSVNG SAARWAQLFQ
RLFEGRAWPA VNIDIHDFGA TPGVVRLRLE QGFEEIAHD