ID   ACON_LEGPH              Reviewed;         891 AA.
AC   P37032; Q5ZUV2;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   04-NOV-2026, entry version 154.
DE   RecName: Full=Aconitate hydratase A {ECO:0000303|PubMed:8366052};
DE            Short=ACN {ECO:0000303|PubMed:8366052};
DE            Short=Aconitase {ECO:0000303|PubMed:8366052};
DE            EC=4.2.1.3 {ECO:0000250|UniProtKB:Q8ZP52};
DE   AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE   AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE   AltName: Full=IP210 {ECO:0000303|PubMed:8366052};
DE   AltName: Full=Iron-responsive protein-like {ECO:0000305|PubMed:8366052};
DE            Short=IRP-like {ECO:0000305|PubMed:8366052};
DE   AltName: Full=Major iron-containing protein {ECO:0000303|PubMed:8366052};
DE            Short=MICP {ECO:0000303|PubMed:8366052};
DE   AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE            EC=4.2.1.99 {ECO:0000250|UniProtKB:Q8ZP52};
DE   AltName: Full=RNA-binding protein {ECO:0000305|PubMed:8366052};
GN   Name=acn; OrderedLocusNames=lpg1690;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Legionellales; Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RX   PubMed=8366052; DOI=10.1128/jb.175.17.5666-5676.1993;
RA   Mengaud J.M., Horwitz M.A.;
RT   "The major iron-containing protein of Legionella pneumophila is an
RT   aconitase homologous with the human iron-responsive element-binding
RT   protein.";
RL   J. Bacteriol. 175:5666-5676(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(2004).
CC   -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC       via the tricarboxylic acid (TCA)(acetyl degradation route) and probably
CC       the 2-methylcitrate cycle I (propionate degradation route). Catalyzes
CC       the reversible isomerization of citrate to isocitrate via cis-
CC       aconitate. The apo form of AcnA functions as a RNA-binding regulatory
CC       protein (PubMed:8366052). Could catalyze the hydration of 2-methyl-cis-
CC       aconitate to yield (2R,3S)-2-methylisocitrate (By similarity).
CC       {ECO:0000250|UniProtKB:Q8ZP52, ECO:0000269|PubMed:8366052}.
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:0000250|UniProtKB:Q8ZP52};
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:0000250|UniProtKB:Q8ZP52};
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}.
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8366052}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; L22081; AAA25295.1; -; Genomic_DNA.
DR   EMBL; AE017354; AAU27770.1; -; Genomic_DNA.
DR   PIR; B48642; B48642.
DR   RefSeq; WP_010947417.1; NC_002942.5.
DR   AlphaFoldDB; P37032; -.
DR   SMR; P37032; -.
DR   STRING; 272624.lpg1690; -.
DR   PaxDb; 272624-lpg1690; -.
DR   GeneID; 57035681; -.
DR   KEGG; lpn:lpg1690; -.
DR   PATRIC; fig|272624.6.peg.1771; -.
DR   eggNOG; COG1048; Bacteria.
DR   HOGENOM; CLU_013476_2_1_6; -.
DR   OMA; AAKEKWP; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000000609; Chromosome.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0003994; F:aconitate hydratase activity; ISS:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR   GO; GO:0019543; P:propionate catabolic process; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR   CDD; cd01586; AcnA_IRP; 1.
DR   CDD; cd01580; AcnA_IRP_Swivel; 1.
DR   FunFam; 3.20.19.10:FF:000001; Aconitate hydratase; 1.
DR   FunFam; 3.30.499.10:FF:000002; Aconitate hydratase; 1.
DR   FunFam; 3.30.499.10:FF:000020; Aconitate hydratase A; 1.
DR   Gene3D; 6.10.190.10; -; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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   NCBIfam; NF006757; acnA; 1.
DR   NCBIfam; NF009520; acnA; 1.
DR   NCBIfam; TIGR01341; aconitase_1; 1.
DR   PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 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_0000076662"
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;  98209 MW;  F81FC99520859B48 CRC64;
     MKVGQDSLST KSQLTVDGKT YNYYSLKEAE NKHFKGINRL PYSLKVLLEN LLRFEDGNTV
     TTKDIKAIAD WLHNKTSQHE IAFRPTRVLM QDFTGVPAVV DLAAMRTAIV KMGGNADKIS
     PLSPVDLVID HSVMVDKFAS ADALEVNTKI EIERNKERYE FLRWGQKAFS NFQVVPPGTG
     ICHQVNLEYL GKTVWNSEND GQLYAYPDTL VGTDSHTTMI NGLGVLGWGV GGIEAEAAML
     GQPVSMLIPE VIGFKLSGKL KEGITATDLV LTVTQMLRKK GVVGKFVEFY GPGLNDLPLA
     DRATISNMAP EYGATCGFFP VDKETIKYLE LTGRDKHTIA LVEAYAKAQG MWYDKDNEEP
     VFTDSLHLDL GSVEPSLAGP KRPQDKVNLS SLPVEFNNFL IEVGKEKEKE KTFAVKNKDF
     QMKHGHVVIA AITSCTNTSN PSVLMAAGLV AKKAIEKGLQ RKPWVKSSLA PGSKVVTDYL
     RHAGLQTYLD QLGFNLVGYG CTTCIGNSGP LPDDISHCVA EHDLVVSSVL SGNRNFEGRV
     HPQVRANWLA SPPLVVAYAL CGTTCSDLSR EPIGQDKEGN DVYLKDIWPS NEEIAAEVAK
     VSGTMFRKEY AEVFKGDAHW QAIQTSSGQT YEWNPDSTYI QHPPFFENLS LKPEPLKPIK
     QAYVLALFGD SITTDHISPA GSIKASSPAG LYLKSKGVDE KDFNSYGSRR GNHEVMMRGT
     FANIRIRNEM TPGQEGGVTR YVPTGETMSI YDAAMRYQEN QQDLVIIAGK EYGTGSSRDW
     AAKGTNLLGV KAVITESFER IHRSNLIGMG ILPLQFKEGT TRKTLKLDGS ERISIEISDK
     LTPGAMVPVT IERQDGDIEK IETLCRIDTA DELEYYKNGG ILQYVLRKIS S
//