ID A0A0E1VK53_STAA3 Unreviewed; 901 AA. AC A0A0E1VK53; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 02-DEC-2020, entry version 31. DE RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275}; DE Short=Aconitase {ECO:0000256|RuleBase:RU361275}; DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275}; GN Name=acnA {ECO:0000313|EMBL:EES93122.1}; GN ORFNames=HMPREF0776_2365 {ECO:0000313|EMBL:EES93122.1}; OS Staphylococcus aureus subsp. aureus USA300_TCH959. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=450394 {ECO:0000313|EMBL:EES93122.1, ECO:0000313|Proteomes:UP000004631}; RN [1] {ECO:0000313|EMBL:EES93122.1, ECO:0000313|Proteomes:UP000004631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCH959 {ECO:0000313|Proteomes:UP000004631}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L., RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A., RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R., RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R., RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P., RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y., RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L., RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis- CC aconitate. {ECO:0000256|RuleBase:RU361275}. 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:0000256|ARBA:ARBA00002737}. 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:0000256|ARBA:ARBA00000118}; 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:0000256|ARBA:ARBA00023501, CC ECO:0000256|RuleBase:RU361275}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|ARBA:ARBA00001966}; CC -!- COFACTOR: CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000256|RuleBase:RU361275}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}. CC -!- PATHWAY: Organic acid metabolism; propanoate degradation. CC {ECO:0000256|ARBA:ARBA00005026}. CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EES93122.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AASB02000234; EES93122.1; -; Genomic_DNA. DR RefSeq; WP_000729744.1; NZ_GG697985.1. DR SMR; A0A0E1VK53; -. DR EnsemblBacteria; EES93122; EES93122; HMPREF0776_2365. DR GeneID; 45574582; -. DR HOGENOM; CLU_013476_2_1_9; -. DR UniPathway; UPA00223; UER00718. DR UniPathway; UPA00946; -. DR Proteomes; UP000004631; Unassembled WGS sequence. DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC. 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:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.19.10; -; 1. DR Gene3D; 3.30.499.10; -; 1. 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 4Fe-4S {ECO:0000256|RuleBase:RU361275}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275}; KW Lyase {ECO:0000256|RuleBase:RU361275, ECO:0000313|EMBL:EES93122.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT DOMAIN 76..570 FT /note="Aconitase" FT /evidence="ECO:0000259|Pfam:PF00330" FT DOMAIN 700..827 FT /note="Aconitase_C" FT /evidence="ECO:0000259|Pfam:PF00694" SQ SEQUENCE 901 AA; 98970 MW; 52998BA940055E5D CRC64; MAANFKEQSK KHFDLNGQSY TYYDLKAVEE QGITKVSNLP 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 SKVVTGYLRD AGLQPYLDDL GFNLVGYGCT TCIGNSGPLL PEIEKAIADE DLLVTSVLSG NRNFEGRIHP LVKANYLASP QLVVAYALAG TVDIDLQNEP 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 //