ID   MADH_MALRU              Reviewed;         366 AA.
AC   O06928;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=ACP-SH:acetate ligase;
DE            EC=6.2.1.35;
DE   AltName: Full=[Acyl-carrier protein]:acetate ligase;
GN   Name=madH;
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, AND CATALYTIC ACTIVITY.
RX   PubMed=8664258; DOI=10.1021/bi952873p;
RA   Berg M., Hilbi H., Dimroth P.;
RT   "The acyl carrier protein of malonate decarboxylase of Malonomonas rubra
RT   contains 2'-(5''-phosphoribosyl)-3'-dephosphocoenzyme A as a prosthetic
RT   group.";
RL   Biochemistry 35:4689-4696(1996).
CC   -!- FUNCTION: Acyl-carrier protein (ACP) acetate ligase of the biotin-
CC       dependent malonate decarboxylase multienzyme complex (EC 7.2.4.4).
CC       Involved in the conversion of the thiol group of the ACP-bound 2'-(5-
CC       phosphoribosyl)-3'-dephospho-CoA prosthetic group into its acetyl
CC       thioester using the energy from the hydrolysis of ATP.
CC       {ECO:0000269|PubMed:8664258}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + holo-[ACP] = acetyl-[ACP] + AMP + diphosphate;
CC         Xref=Rhea:RHEA:31339, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78446, ChEBI:CHEBI:456215;
CC         EC=6.2.1.35; Evidence={ECO:0000269|PubMed:8664258};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR   EMBL; U87980; AAC45404.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06928; -.
DR   KEGG; ag:AAC45404; -.
DR   BioCyc; MetaCyc:MON-14253; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR042099; ANL_N_sf.
PE   1: Evidence at protein level;
KW   Cytoplasm; Ligase.
FT   CHAIN           1..366
FT                   /note="ACP-SH:acetate ligase"
FT                   /id="PRO_0000424277"
SQ   SEQUENCE   366 AA;  40347 MW;  6FA268A84DF2AB92 CRC64;
     MAEQLKELAE MVESFGTAPT MGEMPCRTLA TKGINGPTAA HVIEEIHTPF NLAYVTFTTG
     STAFQNVVGV THSEIDGRVR ASLAAFDMAN VERHGKFLVT YAPLVNVFSA EALKIHGLDW
     FFLQRSSRDA FLLSLCQEKP NVLIGESTFI RSALEDASVL GLSHSIPQGV IAFTAGTPLD
     LDLLQVAEKH NWKIHDLYGC QEFGWLTLDG VPLRADITLI PSPKGSDFRE FVVGGLPMAD
     SFPYAESGHV CNPEGKIITY RRARTNPEYE VIVRETKLSS KETTERVART ILRIKGRVVK
     VDPALKVSST KTVLDLVPSV SAEGKSTSES YRIEGDDKTF LFETLIEAQL ALQQTAKTDQ
     VWKKTR