ID   MADA_MALRU              Reviewed;         554 AA.
AC   O06924;
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=Acetyl-S-ACP:malonate ACP transferase;
DE            Short=ACP transferase;
DE            EC=2.3.1.187;
DE   AltName: Full=Malonate/acetyl-CoA transferase;
GN   Name=madA;
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).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18251085; DOI=10.1007/s002030050100;
RA   Hilbi H., Dimroth P.;
RT   "Purification and characterization of a cytoplasmic enzyme component of the
RT   Na+-activated malonate decarboxylase system of Malonomonas rubra: acetyl-S-
RT   acyl carrier protein: malonate acyl carrier protein-SH transferase.";
RL   Arch. Microbiol. 162:48-56(1994).
CC   -!- FUNCTION: Alpha subunit of the biotin-independent and biotin-dependent
CC       malonate decarboxylase multienzyme complex (EC 4.1.1.88 and EC 7.2.4.4,
CC       respectively). Acts as an acyl-carrier protein (ACP) transferase
CC       component. This first step in malonate decarboxylation involves the
CC       exchange of an acetyl thioester residue bound to the activated ACP
CC       subunit for a malonyl thioester residue. Has a weak activity with
CC       acetyl-CoA as substrate. {ECO:0000269|PubMed:18251085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-[ACP] + malonate = acetate + malonyl-[ACP];
CC         Xref=Rhea:RHEA:17649, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9623,
CC         ChEBI:CHEBI:15792, ChEBI:CHEBI:30089, ChEBI:CHEBI:78446,
CC         ChEBI:CHEBI:78449; EC=2.3.1.187;
CC         Evidence={ECO:0000269|PubMed:18251085};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.5 mM for malonate {ECO:0000269|PubMed:18251085};
CC         KM=1.9 mM for malonyl-CoA {ECO:0000269|PubMed:18251085};
CC         KM=6.9 mM for acetyl-CoA {ECO:0000269|PubMed:18251085};
CC         KM=54 mM for acetate {ECO:0000269|PubMed:18251085};
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:18251085};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR   EMBL; U87980; AAC45400.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06924; -.
DR   SMR; O06924; -.
DR   TCDB; 3.B.1.1.4; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR   KEGG; ag:AAC45400; -.
DR   BioCyc; MetaCyc:MON-14254; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005777; MadA.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF16957; Mal_decarbox_Al; 1.
DR   SUPFAM; SSF100950; SSF100950; 2.
DR   TIGRFAMs; TIGR01110; mdcA; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Transferase.
FT   CHAIN           1..554
FT                   /note="Acetyl-S-ACP:malonate ACP transferase"
FT                   /id="PRO_0000424274"
SQ   SEQUENCE   554 AA;  61148 MW;  D5BB656000482DCC CRC64;
     MQKEKVWDKL STDTEERMNA ANELFSDRKV VPSQNGVALL EAVIRAGDRI NLEGNNQKQA
     DFLAECLGSC DSEKINNLHM VQSAVPLPIH LDIFDKGIAK KLDFAYGGPM AAKVAEFLRE
     GKLELGAIHT YLELFARYFM DLTPRVSLIC AYEGDKDGNL YTGFNTEDTP VIAEATKFRQ
     GIVIAQVNKL VDKVQRVDIP GEWVDAVIES PKPFYLEPLF TRDPANITDT QVLMGMMALK
     GIYGEYGVQR LNHGIGFFTA AIELLLPTYG NELGLKGKIC KHFALNPHPT MIPAIEDGWV
     ESIHSFGGEL GMQKYCEARP DIFFIGPDGS MRSNRAYSQT AGHYATDMFI GGTLQIDKYG
     NSSTATASRV AGFGGAPNMG CDAKGRRHVT DSWLKCGAEF EDQAALLGDM PRGKRLVVQM
     QETFKEKMDP SFVEKLDAWN LAKNANLDLA PVMIYSDDLT HIVTEEGIAY LAKCRGLEER
     MAAIRGVAGY TEVGLSADPK ETKTLRERGI VKTPEDLGID RSRANRSMLA AKSVKDLVDC
     SGGLYEPPAR FVNW