ID   MADD_MALRU              Reviewed;         292 AA.
AC   O06927;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Malonyl-S-ACP:biotin-protein carboxyltransferase MADD;
DE            EC=2.1.3.10;
GN   Name=madD;
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; AAC45403.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06927; -.
DR   SMR; O06927; -.
DR   TCDB; 3.B.1.1.4; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR   KEGG; ag:AAC45403; -.
DR   BioCyc; MetaCyc:MON-14256; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase 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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR009648; Malonate_gamma.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR03134; malonate_gamma; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Transferase.
FT   CHAIN           1..292
FT                   /note="Malonyl-S-ACP:biotin-protein carboxyltransferase
FT                   MADD"
FT                   /id="PRO_0000424276"
FT   DOMAIN          1..281
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ   SEQUENCE   292 AA;  31829 MW;  91D1FB205C318359 CRC64;
     MEIMMGQGRL AIEKIVDPES FKENTIGESS FEDNEVGPGA VVGTAQIGDQ DCTIIASDAM
     AMNERFPVVY AGIIGLEEGY KMAMAVYKTI EADKEKKGTE KRPILLIVDT PGNGPGKQEE
     IFGMNKSTGA YQLALAEARK AGHPIVAMVI GRAISGAFLC HGLQADRILS LSSKFETMIH
     VMPLTSVSVI TKLDIERLEE LSKTNPVFAA GPDFFYQLGG VEELVEEVDG MRSCILKHIA
     EIREMKAAGE EARLGPWGRG ALGEQRGGRM IRGKVMAMMD KQFFAFAEQN LY