ID   ACNA_STAAR              Reviewed;         901 AA.
AC   Q6GH55;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Aconitate hydratase A {ECO:0000250|UniProtKB:Q8ZP52};
DE            Short=ACN {ECO:0000250|UniProtKB:Q8ZP52};
DE            Short=Aconitase {ECO:0000250|UniProtKB:Q8ZP52};
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=Iron-responsive protein-like {ECO:0000250|UniProtKB:P09339};
DE            Short=IRP-like {ECO:0000250|UniProtKB:P09339};
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:0000250|UniProtKB:P09339};
GN   Name=acnA; Synonyms=citB; OrderedLocusNames=SAR1362;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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. Could catalyze the hydration of 2-methyl-cis-aconitate to
CC       yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a
CC       RNA-binding regulatory protein. {ECO:0000250|UniProtKB:P09339,
CC       ECO:0000250|UniProtKB:Q8ZP52}.
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:0000250|UniProtKB:Q8ZP52}.
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000250|UniProtKB:Q8ZP52}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P09339}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; BX571856; CAG40360.1; -; Genomic_DNA.
DR   RefSeq; WP_000729730.1; NC_002952.2.
DR   AlphaFoldDB; Q6GH55; -.
DR   SMR; Q6GH55; -.
DR   KEGG; sar:SAR1362; -.
DR   HOGENOM; CLU_013476_2_1_9; -.
DR   OMA; NGGIMQY; -.
DR   OrthoDB; 363064at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000000596; 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:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
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:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS: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   3: Inferred from homology;
KW   Iron; Iron-sulfur; Lyase; Metal-binding; RNA-binding;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..901
FT                   /note="Aconitate hydratase A"
FT                   /id="PRO_0000076669"
FT   BINDING         443
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P36683"
FT   BINDING         509
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P36683"
FT   BINDING         512
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P36683"
SQ   SEQUENCE   901 AA;  98912 MW;  A7F24AF5E08F9116 CRC64;
     MAANFKEQSK KHFDLNGQSY TYYDLKAVEE QGITKVSKLP YSIRVLLESL LRQEDDFVIT
     DDHIKALSQF GKDGNEGEVP FKPSRVILQD FTGVPAVVDL ASLRKAMDDV GGDITKINPE
     VPVDLVIDHS VQVDSYANPE ALERNMKLEF ERNYERYQFL NWATKAFDNY NAVPPATGIV
     HQVNLEYLAS VVHVRDVDGE KTAFPDTLVG TDSHTTMING IGVLGWGVGG IEAEAGMLGQ
     PSYFPIPEVI GVRLVNSLPQ GATATDLALR VTQELRKKGV VGKFVEFFGP GVQHLPLADR
     ATIANMAPEY GATCGFFPVD DESLKYMKLT GRSDEHIALV KEYLKQNHMF FDVEKEDPNY
     TDVIELDLST VEASLSGPKR PQDLIFLSDM KSSFENSVTA PAGNQGHGLD KSEFDKKAEI
     NFKDGSKATM KTGDIAIAAI TSCTNTSNPY VMLGAGLVAK KAVEKGLKVP EYVKTSLAPG
     SKVVTGYLRG AGLQPYLDDL GFNLVGYGCT TCIGNSGPLL PEIEKAIADE DLLVTSVLSG
     NRNFEGRIHP LVKANYLASP QLVVAYALAG SVDIDLQNEP IGKGNDGEDV YLKDIWPSIK
     EVSDTVDSVV TPELFIEEYN NVYNNNELWN EIDVTDQPLY DFDPNSTYIQ NPSFFQGLSK
     EPGTIVPLNG LRVMGKFGDS VTTDHISPAG AIGKDTPAGK YLQDHQVPIR EFNSYGSRRG
     NHEVMVRGTF ANIRIKNQLA PGTEGGFTTY WPTNEVMPIF DAAMKYKEDG TGLVVLAGND
     YGMGSSRDWA AKGTNLLGVK TVIAQSYERI HRSNLVMMGV LPLEFKKGES ADSLGLDGTE
     EISVNIDENV QPHDYVKVTA KKQDGDLVEF DAMVRFDSLV EMDYYRHGGI LQMVLRNKLA
     Q