ID A0A0E1VK53_STAA3 Unreviewed; 901 AA. AC A0A0E1VK53; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 10-MAY-2017, entry version 16. 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., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via CC cis-aconitate. {ECO:0000256|RuleBase:RU361275}. CC -!- CATALYTIC ACTIVITY: Citrate = isocitrate. CC {ECO:0000256|RuleBase:RU361275}. CC -!- COFACTOR: CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000256|RuleBase:RU361275}; CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. CC {ECO:0000256|RuleBase:RU361275}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 RefSeq; WP_000729744.1; NZ_GG697985.1. DR RefSeq; WP_000729744.1; NZ_GG697985.1. DR ProteinModelPortal; A0A0E1VK53; -. DR SMR; A0A0E1VK53; -. DR EnsemblBacteria; EES93122; EES93122; HMPREF0776_2365. DR OMA; ENLAKWG; -. DR Proteomes; UP000004631; Unassembled WGS sequence. 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:0008152; P:metabolic process; IEA:InterPro. DR Gene3D; 3.20.19.10; -; 1. DR Gene3D; 3.30.499.10; -; 2. DR Gene3D; 3.40.1060.10; -; 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; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR006249; Aconitase/IRP2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. 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; SSF52016; SSF52016; 1. 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 Complete proteome {ECO:0000313|Proteomes:UP000004631}; KW Iron {ECO:0000256|RuleBase:RU361275}; KW Iron-sulfur {ECO:0000256|RuleBase:RU361275}; KW Lyase {ECO:0000256|RuleBase:RU361275, ECO:0000256|SAAS:SAAS00638284, KW ECO:0000313|EMBL:EES93122.1}; KW Metal-binding {ECO:0000256|RuleBase:RU361275}. FT DOMAIN 76 570 Aconitase. {ECO:0000259|Pfam:PF00330}. FT DOMAIN 700 827 Aconitase_C. {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 //