ID   ACNA_SALTY              Reviewed;         891 AA.
AC   Q8ZP52;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Aconitate hydratase A {ECO:0000303|PubMed:11294638};
DE            Short=ACN {ECO:0000303|PubMed:11294638};
DE            Short=Aconitase {ECO:0000303|PubMed:11294638};
DE            EC=4.2.1.3 {ECO:0000269|PubMed:11294638};
DE   AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000305|PubMed:11294638};
DE   AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000305|PubMed:11294638};
DE   AltName: Full=2-methyl-cis-aconitate hydratase {ECO:0000303|PubMed:11294638};
DE            EC=4.2.1.99 {ECO:0000269|PubMed:11294638};
DE   AltName: Full=Iron-responsive protein-like {ECO:0000250|UniProtKB:P09339};
DE            Short=IRP-like {ECO:0000250|UniProtKB:P09339};
DE   AltName: Full=RNA-binding protein {ECO:0000250|UniProtKB:P09339};
GN   Name=acnA; OrderedLocusNames=STM1712;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND SUBSTRATE
RP   SPECIFICITY.
RX   PubMed=11294638; DOI=10.1021/bi015503b;
RA   Horswill A.R., Escalante-Semerena J.C.;
RT   "In vitro conversion of propionate to pyruvate by Salmonella enterica
RT   enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase enzymes catalyze
RT   the conversion of 2-methylcitrate to 2-methylisocitrate.";
RL   Biochemistry 40:4703-4713(2001).
CC   -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC       via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-
CC       methylcitrate cycle I (propionate degradation route). Catalyzes the
CC       reversible isomerization of citrate to isocitrate via cis-aconitate.
CC       Also catalyzes the hydration of 2-methyl-cis-aconitate to yield
CC       (2R,3S)-2-methylisocitrate. The (2S,3S)-2-methylcitrate (2-MC) is a
CC       very poor substrate (PubMed:11294638). The apo form of AcnA functions
CC       as a RNA-binding regulatory protein (By similarity).
CC       {ECO:0000250|UniProtKB:P09339, ECO:0000269|PubMed:11294638}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC         ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC         Evidence={ECO:0000269|PubMed:11294638};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC         aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC         Evidence={ECO:0000269|PubMed:11294638};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P09339};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:P09339};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 2/2. {ECO:0000305|PubMed:11294638}.
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000305|PubMed:11294638}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P09339}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show no phenotype during
CC       growth on propionate, acetate, succinate, glycerol and glucose. The
CC       acnAB double mutant does not grow on propionate even when supplemented
CC       with glutamate and is unable to respire propionate under anaerobic
CC       growth conditions. {ECO:0000269|PubMed:11294638}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AE006468; AAL20630.1; -; Genomic_DNA.
DR   RefSeq; NP_460671.1; NC_003197.2.
DR   RefSeq; WP_000099475.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZP52; -.
DR   SMR; Q8ZP52; -.
DR   STRING; 99287.STM1712; -.
DR   PaxDb; Q8ZP52; -.
DR   PRIDE; Q8ZP52; -.
DR   EnsemblBacteria; AAL20630; AAL20630; STM1712.
DR   GeneID; 1253231; -.
DR   KEGG; stm:STM1712; -.
DR   PATRIC; fig|99287.12.peg.1807; -.
DR   HOGENOM; CLU_013476_2_1_6; -.
DR   OMA; NGGIMQY; -.
DR   PhylomeDB; Q8ZP52; -.
DR   BioCyc; MetaCyc:MON-65; -.
DR   BioCyc; SENT99287:STM1712-MON; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0003994; F:aconitate hydratase activity; IDA:UniProtKB.
DR   GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030350; F:iron-responsive element binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IDA:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IDA:UniProtKB.
DR   CDD; cd01580; AcnA_IRP_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 2.
DR   InterPro; IPR044137; AcnA_IRP_Swivel.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR006249; Aconitase/IRP2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   PANTHER; PTHR11670; PTHR11670; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR01341; aconitase_1; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW   RNA-binding; Tricarboxylic acid cycle.
FT   CHAIN           1..891
FT                   /note="Aconitate hydratase A"
FT                   /id="PRO_0000432980"
FT   BINDING         435
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P36683"
FT   BINDING         501
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P36683"
FT   BINDING         504
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P36683"
SQ   SEQUENCE   891 AA;  97502 MW;  EF0A3A2F96890FFE CRC64;
     MSSTLREASK DTLQAKDKTY HYYSLPLAAK SLGDIARLPK SLKVLLENLL RWQDGESVTD
     EDIQALAGWL KNAHADREIA WRPARVLMQD FTGVPAVVDL AAMREAVKRL GGDTSKVNPL
     SPVDLVIDHS VTVDHFGDDD AFEENVRLEM ERNHERYMFL KWGKQAFSRF SVVPPGTGIC
     HQVNLEYLGK AVWSELQDGE WIAYPDSLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
     PVSMLIPDVV GFKLTGKLRE GITATDLVLT VTQMLRKHGV VGKFVEFYGD GLDSLPLADR
     ATIANMSPEY GATCGFFPID AITLEYMRLS GRSDDLVELV ETYAKAQGMW RNPGDEPVFT
     STLELDMGDV EASLAGPKRP QDRVALGDVP KAFAASAELE LNTAQRDRQP VDYTMNGQPY
     QLPDGAVVIA AITSCTNTSN PSVLMAAGLL AKKAVTLGLK RQPWVKASLA PGSKVVSDYL
     AQAKLTPYLD ELGFNLVGYG CTTCIGNSGP LPEPIETAIK KGDLTVGAVL SGNRNFEGRI
     HPLVKTNWLA SPPLVVAYAL AGNMNINLAT DPLGYDRKGD PVYLKDIWPS AQEIARAVEL
     VSSDMFRKEY AEVFEGTEEW KSIQVESSDT YGWQSDSTYI RLSPFFDEMQ AQPAPVKDIH
     GARILAMLGD SVTTDHISPA GSIKPDSPAG RYLQNHGVER KDFNSYGSRR GNHEVMMRGT
     FANIRIRNEM LPGVEGGMTR HLPGTEAMSI YDAAMLYQQE KTPLAVIAGK EYGSGSSRDW
     AAKGPRLLGI RVVIAESFER IHRSNLIGMG ILPLEFPQGV TRKTLGLTGE EVIDIADLQN
     LRPGATIPVT LTRSDGSKET VPCRCRIDTA TELTYYQNDG ILHYVIRNML N