| IED ID | IndEnz0002013966 |
| Enzyme Type ID | protease013966 |
| Protein Name |
Aconitate hydratase B ACN Aconitase EC 4.2.1.3 2R,3S -2-methylisocitrate dehydratase 2S,3R -3-hydroxybutane-1,2,3-tricarboxylate dehydratase 2-methyl-cis-aconitate hydratase EC 4.2.1.99 Iron-responsive protein-like IRP-like RNA-binding protein |
| Gene Name | acnB STM0158 |
| Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhimurium Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Enzyme Sequence | MLEEYRKHVAERAAQGIVPKPLDATQMAALVELLKTPPVGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAVAKGDTTSPLVSPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLSRPPLAEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHAQAMLKNAREGIEPDQPGVVGPIKQIEALQKKGYPLAYVGDVVGTGSSRKSATNSVLWFMGDDIPNVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNHETGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESSRGFSLAQKMVGRACGVKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVTTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIVEYLTSNIVLLKWMIAEGYGDRRTLERRIQGMEKWLADPQLLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARLLSDVQGEKIDEVFIGSCMTNIGHFRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTGANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDTYRYLNFDQLSQYTEKADGVIFQTAV |
| Enzyme Length | 865 |
| Uniprot Accession Number | Q8ZRS8 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 191; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36683; BINDING 498; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36683; BINDING 791; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36683; BINDING 796; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36683 |
| 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:11294638}; CATALYTIC ACTIVITY: Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377, ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99; Evidence={ECO:0000269|PubMed:11294638}; |
| DNA Binding | |
| EC Number | 4.2.1.3; 4.2.1.99 |
| Enzyme Function | FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein which regulates FliC synthesis via interaction with the ftsH transcript to decrease the intracellular levels of FtsH. The lower levels of FtsH protease activity then influence sigma-32, DnaK and ultimately FliC production. {ECO:0000269|PubMed:11294638, ECO:0000269|PubMed:15009904}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. {ECO:0000305|PubMed:11294638}.; PATHWAY: Organic acid metabolism; propanoate degradation. {ECO:0000305|PubMed:11294638}. |
| nucleotide Binding | |
| Features | Binding site (4); Chain (1); Metal binding (3); Region (2) |
| Keywords | 4Fe-4S;Iron;Iron-sulfur;Lyase;Metal-binding;RNA-binding;Reference proteome;Tricarboxylic acid cycle |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 23637460; |
| Motif | |
| Gene Encoded By | |
| Mass | 93,529 |
| Kinetics | |
| Metal Binding | METAL 710; /note=Iron-sulfur (4Fe-4S); /evidence=ECO:0000250|UniProtKB:P36683; METAL 769; /note=Iron-sulfur (4Fe-4S); /evidence=ECO:0000250|UniProtKB:P36683; METAL 772; /note=Iron-sulfur (4Fe-4S); /evidence=ECO:0000250|UniProtKB:P36683 |
| Rhea ID | RHEA:10336; RHEA:17941 |
| Cross Reference Brenda |