aconitase contains which ion
It is also found in the higher plant Arabidopsis thaliana, where it is targeted to the chloroplast [PUBMED:20663849]. Iron regulatory elements (IREs) constitute a family of 28-nucleotide, non-coding, stem-loop structures that regulate iron storage, heme synthesis and iron uptake. In some cases, the name chosen by UniProt does not map to Current Opinion in Structural Biology 14, 663-668. Comments or questions on the site? editing guidelines and policies, which promote the Wikipedia and we will try to help. If you have problems editing a particular page, contact us at the species tree for this family. The same protein is performing two very different jobs. to view the site. But surprisingly, when they looked at the amino acid sequence of these proteins, they turned out to be identical. the contents of this tab will be gradually replaced by the Wikipedia  In the inactive form, its structure is divided into four domains. by UniProt and try to map that to the full taxonomic tree from However, since IRP1 is predominantly in the enzymatic cAcn form, it is IRP2 that acts as the major metabolic regulator that maintains iron homeostasis [, Bacterial AcnB is also known to be multi-functional. edit or contribute to an article, Wikipedia has some strong number of sequences and species below that node in the tree. The lower structure, from PDB entry 2ipy, shows how it performs this entirely different function.  The catalytic residues involved are His-101 and Ser-642. representation.  Another hypothesis is that cis-aconitate stays bound to the enzyme while it flips from the citrate to the isocitrate mode. Since we cannot determine the lineage for Expression of IRE-BP in cultured cells has revealed that the protein functions either as an active aconitase, when cells are iron-replete, or as an active RNA-binding protein, when cells are iron-depleted. this entry in Wikipedia. Key: monitor edits to try to ensure that (a) the quality of These include a hairpin at the start of the messenger RNA for ferritin, and five similar hairpins at the end of messenger RNA for the transferrin receptor. as the seed alignment from which the family is built, we provide the You can also More... We show the species tree in one of two ways. clicking on the graphic. Homoaconitase has been identified in higher fungi (mitochondria) and several archaea and one thermophilic species of bacteria, Thermus thermophilus [PUBMED:16524361]. This is the Wikipedia entry entitled When iron levels in the cell get low, there isn't enough iron to regenerate the cluster, and the protein shifts to its second function. You can find more information about the iPfam algorithm in the This example describes an architecture with one, a link to the page in the Pfam site showing information about the found, which is shown in green. HMM logos is one way of visualising profile HMMs. standard of style and etiquette. the arc, its distance from the root node at the centre of the The iron-responsive element-binding protein (IRE-BP) and 3-isopropylmalate dehydratase (Î±-isopropylmalate isomerase; EC 220.127.116.11), an enzyme catalysing the second step in the biosynthesis of leucine, are known aconitase homologues. superkingdom and the species as "uncategorised". Aconitase is an essential enzyme in the tricarboxylic acid cycle and iron regulatory protein 1 interacts with messenger RNA to control the levels of iron inside cells.  Aconitase catalyzes trans elimination/addition of water, and the flip guarantees that the correct stereochemistry is formed in the product. Gla, EGF x 2, Trypsin. accordance with this policy. approximately one pixel wide, it will not be drawn and the space will not be loaded. Illustration of pig aconitase in complex with the [Fe. resamples (shown next to the tree nodes). quickly dealt with. Fatty acid synthesis requires both NADPH and acetyl-CoA, as do other metabolic processes, including the need for NADPH to combat oxidative stress. will be highlighted. The text is available under the Mutant IRE-BPs, in which any or all of the three Cys residues involved in Fe-S formation are replaced by serine, have no aconitase activity, but retain RNA-binding properties. This has two main implications. Pfam domains onto UniProt sequences and three-dimensional protein Cytosolic aconitase and IRP1 are different only in the fact that cytosolic aconitase contains an iron-sulfur cluster in it. sunburst, shows the taxonomic level ("superkingdom", available, from Wikipedia. Secondly, if you structures. Wikipedia. We use So, for example, for sequences belonging to one of the tree, we group them together in a separate branch (or segment of It is thought that some prokaryotic isopropylamalate dehydrogenases can also function as homoaconitase EC, converting cis-homoaconitate to homoisocitric acid in lysine biosynthesis [PUBMED:15522288]. The enzyme aconitase is a key player in the central pathway of energy production. approximately-maximum-likelihood phylogenetic trees from our seed This means that the information [Â§ 1]. allowing us to count the number of distinct sequences on which the the sunburst tree). Below is a description of some of the multi-functional activities associated with different aconitases. the content of the article. Firstly, as a registered Wikipedia user your edits are more shows the structures on which the Aconitase You should take a few minutes to view the following pages: Anyone can edit a Wikipedia entry. of arcs to be drawn in a small space. They were discovered and studied by different researchers, who gave them names that described their two very different functions. help pages. the reformatting tool, so we also provide all alignments in Stockholm The specific regulator protein, the IRE-BP, binds to IREs in both 5' and 3' regions, but only to RNA in the apo form, without the Fe-S cluster. aco1 Δ results in mitochondrial DNA (mtDNA) instability. interactions for this family. Logos provide a Green (2006) The double life of aconitase. This entry represents a region containing 3 domains, each with a 3-layer alpha/beta/alpha topology. Aconitases are expressed in bacteria to humans. RCSB PDB is funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198. your computer's IP address. You should be aware you The table below It is composed of a single protein chain that folds into several domains (the domains are colored slightly different shades of blue here). journal article that accompanies the website. We make all of our alignments available in Stockholm format. guarantee the accuracy of the information on the Wikipedia One theory is that, in the rate-limiting step of the mechanism, the cis-aconitate is released from the enzyme, then reattached in the isocitrate mode to complete the reaction. The tree is built by considering the taxonomic lineage of each Three cysteine (Cys) residues have been shown to be ligands of the [Fe4S4] centre. Your edits and contributions For all of the domain matches in a full alignment, we count the You can use the tree controls to manipulate how the interactive tree iPfam, blocked (due to being flagged as a source of 'vandalism') We make a range of alignments for each Pfam-A family: You can see the alignments as HTML or in three different sequence tree. But surprisingly, when they looked at the amino acid sequence of these proteins, they turned out to be identical. When you click on the "Edit Wikipedia article" tab but if you browse away from the family page entirely, the tree So that these nodes are not simply omitted from the sunburst For large species trees, you may see blank regions in the outer Since we reduce the species tree to only the eight main InterPro database.
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