ID   ACNA_STAES              Reviewed;         901 AA.
AC   Q8CPC2;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=SE_1032;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04629.1; -; Genomic_DNA.
DR   RefSeq; NP_764587.1; NC_004461.1.
DR   RefSeq; WP_002456207.1; NZ_WBME01000040.1.
DR   AlphaFoldDB; Q8CPC2; -.
DR   SMR; Q8CPC2; -.
DR   STRING; 176280.SE_1032; -.
DR   EnsemblBacteria; AAO04629; AAO04629; SE_1032.
DR   KEGG; sep:SE_1032; -.
DR   PATRIC; fig|176280.10.peg.1007; -.
DR   eggNOG; COG1048; Bacteria.
DR   HOGENOM; CLU_013476_2_1_9; -.
DR   OMA; NGGIMQY; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000001411; 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_0000076672"
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;  99287 MW;  E94F6B620AFAA38A CRC64;
     MASNIKEQAK KQFELNGQSY TYYDLQTLEE KGLAKISKLP YSIRVLLESV LRQEDDFVIT
     DDHIKALSKF GNAGNEGEVP FKPSRVILQD FTGVPAVVDL ASLRKAMNDV GGDINKINPE
     VPVDLVIDHS VQVDSYANPE ALERNMKLEF ERNYERYQFL NWATKAFDNY NAVPPATGIV
     HQVNLEYLAN VVHVRDVDGE KTAFPDTLVG TDSHTTMING IGVLGWGVGG IEAEAGMLGQ
     PSYFPIPEVI GVRLTHSLPQ GSTATDLALR VTEELRKKGV VGKFVEFFGP GVQHLPLADR
     ATIANMAPEY GATCGFFPVD EESLKYMKLT GRDEEHIELV KEYLQQNHMF FDVEKEDPEY
     TDVIDLDLST VEASLSGPKR PQDLIFLSDM KKEFEKSVTA PAGNQGHGLD QSEFDKKAEI
     NFNDGSKATM KTGDIAIAAI TSCTNTSNPY VMLGAGLVAK KAVEKGLKVP EFVKTSLAPG
     SKVVTGYLRD SGLQQYLDDL GFNLVGYGCT TCIGNSGPLL PEIEKAVADE DLLVTSVLSG
     NRNFEGRIHP LVKANYLASP QLVVAYALAG TVDIDLQNEP IGKGKDGKDV YLQDIWPSIQ
     EVSDTVDKVV TPELFLEEYK NVYHNNEMWN EIDVTDEPLY DFDPNSTYIQ NPTFFQGLSK
     EPGKIEPLKS LRVMGKFGDS VTTDHISPAG AIGKDTPAGK YLLDHDVAIR NFNSYGSRRG
     NHEVMVRGTF ANIRIKNQLA PGTEGGFTTY WPTGEIMPIY DAAMKYKEDG TGLVVLAGND
     YGMGSSRDWA AKGTNLLGVK TVIAQSYERI HRSNLVMMGV LPLQFQQGES AEALGLDGKE
     EISVDINEDV QPHDLVNVTA KKENGEIINF KAIVRFDSLV ELDYYRHGGI LQMVLRNKLA
     Q