ID ACON1_PSEAE Reviewed; 910 AA. AC Q9I3F5; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 25-JAN-2012, entry version 64. DE RecName: Full=Aconitate hydratase 1; DE Short=Aconitase 1; DE EC=4.2.1.3; DE AltName: Full=Citrate hydro-lyase 1; GN Name=acnA; OrderedLocusNames=PA1562; OS Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG OS 12228). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via CC cis-aconitate (By similarity). CC -!- CATALYTIC ACTIVITY: Citrate = isocitrate. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity). CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC isocitrate from oxaloacetate: step 2/2. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. 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; AE004091; AAG04951.1; -; Genomic_DNA. DR PIR; B83451; B83451. DR RefSeq; NP_250253.1; NC_002516.2. DR HSSP; P21399; 2B3Y. DR ProteinModelPortal; Q9I3F5; -. DR GeneID; 879412; -. DR GenomeReviews; AE004091_GR; PA1562. DR KEGG; pae:PA1562; -. DR NMPDR; fig|208964.1.peg.1563; -. DR PATRIC; 19837464; VBIPseAer58763_1618. DR PseudoCAP; PA1562; -. DR HOGENOM; HBG289738; -. DR OMA; YSKAQGM; -. DR ProtClustDB; PRK12881; -. DR BioCyc; PAER208964:PA1562-MONOMER; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003994; F:aconitate hydratase activity; IEA:EC. DR GO; GO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC. DR GO; GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR006249; Aconitase/Fe_reg_prot_2. DR InterPro; IPR015934; Aconitase/Fe_reg_prot_2/AcnD. DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl. DR Gene3D; G3DSA:3.30.499.10; Acnase/IPM_dHydase_lsu_aba_1/3; 3. DR Gene3D; G3DSA:3.20.19.10; Aconitase/3IPM_dehydase_swvl; 1. DR Gene3D; G3DSA:3.40.1060.10; Aconitase/IPMdHydase_lsu_aba_2; 1. DR KO; K01681; -. DR PANTHER; PTHR11670; Aconitase-like_core; 1. DR PANTHER; PTHR11670:SF1; Aconitase/Fe_reg_prot_2/AcnD; 1. DR Pfam; PF00330; Aconitase; 2. DR Pfam; PF00694; Aconitase_C; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF52016; Aconitase/3IPM_dehydase_swvl; 1. DR SUPFAM; SSF53732; Aconitase_N; 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; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1 910 Aconitate hydratase 1. FT /FTId=PRO_0000287739. FT METAL 454 454 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 520 520 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 523 523 Iron-sulfur (4Fe-4S) (By similarity). SQ SEQUENCE 910 AA; 99148 MW; C65F23CDB6FA0E1C CRC64; MPALDSLKTL RSLAVDGKTY HYYSLPEAAR TLGDLGKLPM SLKVLLENLL RWEDGSTVTG DDLKALAGWL RERRSDREIQ YRPARVLMQD FTGVPAVVDL AAMRAAMAKA GGDPQKINPL SPVDLVIDHS VMVDKFASES AFEQNVEIEM QRNGERYAFL RWGQNAFDNF SVVPPGTGIC HQVNLEYLGR TVWTKDEDGR TYAFPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ PVSMLIPEVI GFKLTGKLRE GITATDLVLT VTQMLRKKGV VGKFVEFYGD GLADLPLADR ATIANMAPEY GATCGFFPVD EITLGYLRLS GRPESTVKLV EAYSKEQGLW REKGHEPVFT DTLHLDMGEV EASLAGPKRP QDRVALQNVA SAFNEFLGLQ LHPSSTEEGR LLSEGGGGTA VGANAAFGEI DYQHDGQTHR LKNGAVVIAA ITSCTNTSNP SVMMAAGLLA KKAVEKGLQR KPWVKSSLAP GSKVVTDYFK AAGLTRYLDE LGFDLVGYGC TTCIGNSGPL LEPIEKAIQQ ADLTVASVLS GNRNFEGRVH PLVKTNWLAS PPLVVAYALA GSVRINLSEE PLGTGKDGQP VYLKDIWPSQ KEIAEAIQKV DTEMFHKEYA EVFAGDEKWQ AIQVPQSDTY EWQADSTYIQ HPPFFEHIAE APPAIADVEQ ARVLAVLGDS VTTDHISPAG NIKADSPAGR YLREHGVEPK DFNSYGSRRG NHEVMMRGTF ANIRIKNEML GGEEGGNTLY VPSGEKLAIY DAAMRYQEDG TPLVIVAGKE YGTGSSRDWA AKGTNLLGVK AVIAESFERI HRSNLVGMGV LPLQFENGQD RKSLKLTGKE VLNIRGLGGE LKPHMPLSVE VTREDGSQDS FKVLCRIDTL NEVEYFKAGG ILHYVLRSML //