ID Q9I3F5_PSEAE PRELIMINARY; PRT; 910 AA. AC Q9I3F5; DT 01-MAR-2001 (TrEMBLrel. 16, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE Aconitate hydratase 1. GN Name=acnA; OrderedLocusNames=PA1562; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 15692 / PAO1; 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 between 2-isopropylmalate CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate (By CC similarity). CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmaleate + H(2)O. CC -!- CATALYTIC ACTIVITY: (2S)-2-isopropylmaleate + H(2)O = 3-hydroxy-4- CC methyl-3-carboxypentanoate. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2. CC -!- PATHWAY: Tricarboxylic acid cycle. 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; AE004584; AAG04951.1; -. DR PIR; B83451; B83451. DR HSSP; P16276; 1B0J. DR GO; GO:0003994; F:aconitate hydratase activity; IEA. DR GO; GO:0005506; F:iron ion binding; IEA. DR GO; GO:0016829; F:lyase activity; IEA. DR GO; GO:0003723; F:RNA binding; IEA. DR GO; GO:0009098; P:leucine biosynthesis; IEA. DR GO; GO:0008152; P:metabolism; IEA. DR InterPro; IPR006249; Aconitase_1. DR InterPro; IPR000573; Aconitase_C. DR InterPro; IPR001030; Aconitase_N. DR Pfam; PF00330; Aconitase; 1. DR Pfam; PF00694; Aconitase_C; 1. DR PRINTS; PR00415; ACONITASE. DR ProDom; PD000511; Aconitase_N; 1. DR TIGRFAMs; TIGR01341; aconitase_1; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. KW 4Fe-4S; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Leucine biosynthesis; Metal-binding. SQ SEQUENCE 910 AA; 99147 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 //