| IED ID | IndEnz0004000257 |
| Enzyme Type ID | xylanase000257 |
| Protein Name |
Aconitate hydratase A ACN Aconitase EC 4.2.1.3 Aconitate/2-methylaconitate hydratase EC 4.2.1.- Iron-responsive protein-like IRP-like RNA-binding protein |
| Gene Name | citB BSU18000 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MANEQKTAAKDVFQARKTFTTNGKTYHYYSLKALEDSGIGKVSKLPYSIKVLLESVLRQVDGFVIKKEHVENLAKWGTAELKDIDVPFKPSRVILQDFTGVPAVVDLASLRKAMAAVGGDPDKINPEIPVDLVIDHSVQVDKAGTEDALAVNMDLEFERNAERYKFLSWAKKAFNNYQAVPPATGIVHQVNLEFLASVVHAIEEDGELVTYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPVPEVIGAKLVGKLPNGTTATDLALKVTQVLREKGVVGKFVEFFGPGIAELPLADRATIANMAPEYGATCGFFPVDEEALNYLRLTGRDPEHIDVVEAYCRSNGLFYTPDAEDPQFTDVVEIDLSQIEANLSGPKRPQDLIPLSAMQETFKKQLVSPAGNQGFGLNAEEENKEIKFKLLNGEETVMKTGAIAIAAITSCTNTSNPYVLIGAGLVAKKAVELGLKVPNYVKTSLAPGSKVVTGYLVNSGLLPYMKELGFNLVGYGCTTCIGNSGPLSPEIEEAVAKNDLLITSVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGTVNINLKTDPIGVGKDGQNVYFNDIWPSMDEINALVKQTVTPELFRKEYETVFDDNKRWNEIETTDEALYKWDNDSTYIQNPPFFEEMSVEPGKVEPLKGLRVVGKFGDSVTTDHISPAGAIGKDTPAGKYLQEKGVSPRDFNSYGSRRGNHEVMMRGTFANIRIKNQIAPGTEGGFTTYWPTGEVTSIYDACMKYKEDKTGLVVLAGKDYGMGSSRDWAAKGTNLLGIRTVIAESFERIHRSNLVFMGVLPLQFKQGENADTLGLTGKEVIEVDVDETVRPRDLVTVRAINEDGNVTTFEAVVRFDSEVEIDYYRHGGILQMVLREKMKQS |
| Enzyme Length | 909 |
| Uniprot Accession Number | P09339 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000269|PubMed:23354745}; CATALYTIC ACTIVITY: Reaction=3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O; Xref=Rhea:RHEA:57500, ChEBI:CHEBI:15377, ChEBI:CHEBI:57872, ChEBI:CHEBI:141790; Evidence={ECO:0000269|PubMed:28956599}; |
| DNA Binding | |
| EC Number | 4.2.1.3; 4.2.1.- |
| Enzyme Function | FUNCTION: Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles (PubMed:28956599). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate (PubMed:3110133, PubMed:23354745). Also catalyzes the rehydration of 2-methyl-cis-aconitate to produce 2-methylisocitrate (PubMed:28956599). The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role in the regulation of citrate concentration and in the sporulation. To prevent the accumulation of excessive levels of citrate, it binds near the 5' end of the citZ mRNA, decreasing its stability and thereby limiting the concentration of citrate synthase in the cell. Aconitase also binds to the gerE transcript late in sporulation and stabilizes it for translation, thereby increasing the rate and level of GerE protein accumulation (PubMed:10468622, PubMed:16923907, PubMed:23354745, PubMed:9393699). {ECO:0000269|PubMed:10468622, ECO:0000269|PubMed:16923907, ECO:0000269|PubMed:23354745, ECO:0000269|PubMed:28956599, ECO:0000269|PubMed:3110133, ECO:0000269|PubMed:9393699}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. {ECO:0000305|PubMed:23354745}. |
| nucleotide Binding | |
| Features | Chain (1); Initiator methionine (1); Metal binding (3); Mutagenesis (2); Sequence conflict (2) |
| Keywords | Direct protein sequencing;Iron;Iron-sulfur;Lyase;Metal-binding;RNA-binding;Reference proteome;Tricarboxylic acid cycle |
| Interact With | |
| Induction | INDUCTION: By citrate via CcpC. When citrate is absent, CcpC binds to the sites near the citB promoter and blocks expression. When citrate is present, it causes a change in the interaction of CcpC with its binding sites, resulting in derepression of citB. When citrate is very abundant, CcpC activates citB expression, presumably reflecting a change in the interaction of CcpC with RNA polymerase. Also induced by decoyinine and nutrient depletion. {ECO:0000269|PubMed:23139400}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 22512862; |
| Motif | |
| Gene Encoded By | |
| Mass | 99,334 |
| Kinetics | |
| Metal Binding | METAL 450; /note=Iron-sulfur (4Fe-4S); /evidence=ECO:0000250|UniProtKB:P36683; METAL 516; /note=Iron-sulfur (4Fe-4S); /evidence=ECO:0000250|UniProtKB:P36683; METAL 519; /note=Iron-sulfur (4Fe-4S); /evidence=ECO:0000250|UniProtKB:P36683 |
| Rhea ID | RHEA:10336; RHEA:57500 |
| Cross Reference Brenda | 4.2.1.3; |