ID   MADC_MALRU              Reviewed;         318 AA.
AC   O06926;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Malonyl-S-ACP:biotin-protein carboxyltransferase MADC;
DE            EC=2.1.3.10;
GN   Name=madC;
OS   Malonomonas rubra.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Malonomonas.
OX   NCBI_TaxID=57040;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=9128730; DOI=10.1111/j.1432-1033.1997.00103.x;
RA   Berg M., Hilbi H., Dimroth P.;
RT   "Sequence of a gene cluster from Malonomonas rubra encoding components of
RT   the malonate decarboxylase Na+ pump and evidence for their function.";
RL   Eur. J. Biochem. 245:103-115(1997).
CC   -!- FUNCTION: Gamma subunit of the biotin-dependent malonate decarboxylase
CC       multienzyme complex (EC 7.2.4.4). The two subunits MADC and MADD are
CC       required for the transfer of the malonate carboxy group from the acyl-
CC       carrier protein (ACP) to the prosthetic group of the biotin carrier
CC       MADF. Required for the regeneration of ACP.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=malonyl-[ACP] + N(6)-biotinyl-L-lysyl-[protein] = acetyl-[ACP]
CC         + N(6)-carboxybiotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:23028,
CC         Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:78446, ChEBI:CHEBI:78449,
CC         ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.10;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR   EMBL; U87980; AAC45402.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06926; -.
DR   SMR; O06926; -.
DR   TCDB; 3.B.1.1.4; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR   KEGG; ag:AAC45402; -.
DR   BioCyc; MetaCyc:MON-14255; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR017556; Malonate_beta.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR03133; malonate_beta; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   CHAIN           2..318
FT                   /note="Malonyl-S-ACP:biotin-protein carboxyltransferase
FT                   MADC"
FT                   /id="PRO_5000145253"
FT   DOMAIN          2..257
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
SQ   SEQUENCE   318 AA;  34900 MW;  0E9BE42EB7FFC2B9 CRC64;
     MAKWTELQDK SFLEATARER AVGIVDEGTF TEFCGPFDKI YSPHLPLMGE AIEYDDGLVA
     GVGKIGKKPI FVISQEGRFI GGSIGEVSGA KMVKTIQLAS DLYEEMVSEK PDLPEEMRPA
     VVISFETGGV RLHEANAGLL AHAEVMDQIQ NCRGRVPIIS LIGSRVGCFG GMGFVAAATD
     VIIMSQFGRL GLTGPEVIEQ EMGKDEFDAS DRALVYRTTG GKHKYIIGDC NYLAADSIRS
     FRETTTAVLQ KPMEEIETFR RIGSMEKIKE QIELVKLSVS LKPKDSMDVW AHAGNENPES
     LINMTLDEFL AQAKRLKA