ID ACNA_PSEAE Reviewed; 910 AA. AC Q9I3F5; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 08-MAY-2019, entry version 109. 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; OrderedLocusNames=PA1562; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / OS JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1). 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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX 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: Involved in the catabolism of short chain fatty acids CC (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) CC and probably the 2-methylcitrate cycle I (propionate degradation CC route). Catalyzes the reversible isomerization of citrate to CC isocitrate via cis-aconitate. Could catalyze the hydration of 2- CC methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo CC form of AcnA functions as a RNA-binding regulatory protein. CC {ECO:0000250|UniProtKB:P09339, ECO:0000250|UniProtKB:Q8ZP52}. CC -!- CATALYTIC ACTIVITY: CC Reaction=citrate = isocitrate; Xref=Rhea:RHEA:10336, CC ChEBI:CHEBI:16087, 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- CC cis-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; CC isocitrate from oxaloacetate: step 2/2. CC {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}. 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 RefSeq; WP_003105996.1; NZ_QZGE01000003.1. DR SMR; Q9I3F5; -. DR PaxDb; Q9I3F5; -. DR PRIDE; Q9I3F5; -. DR EnsemblBacteria; AAG04951; AAG04951; PA1562. DR GeneID; 879412; -. DR KEGG; pae:PA1562; -. DR PATRIC; fig|208964.12.peg.1618; -. DR PseudoCAP; PA1562; -. DR eggNOG; ENOG4107QM5; Bacteria. DR eggNOG; COG1048; LUCA. DR HOGENOM; HOG000025703; -. DR InParanoid; Q9I3F5; -. DR KO; K01681; -. DR OMA; RDFTQEG; -. DR PhylomeDB; Q9I3F5; -. DR BioCyc; PAER208964:G1FZ6-1591-MONOMER; -. DR UniPathway; UPA00223; UER00718. DR UniPathway; UPA00946; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005737; C:cytoplasm; ISS:PseudoCAP. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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:0005506; F:iron ion binding; ISS:PseudoCAP. DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB. DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB. DR GO; GO:0009061; P:anaerobic respiration; ISS:PseudoCAP. DR GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central. DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; ISS:PseudoCAP. DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB. 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; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW Reference proteome; RNA-binding; Tricarboxylic acid cycle. FT CHAIN 1 910 Aconitate hydratase A. FT /FTId=PRO_0000287739. FT METAL 454 454 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P36683}. FT METAL 520 520 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P36683}. FT METAL 523 523 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P36683}. 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 //