| General Information |
| MoonProt ID | 234 |
| First appeared in release | 1.0 |
| Name(s) | Aconitase
Cytoplasmic aconitate hydratase
Citrate hydro-lyase
Ferritin repressor protein
Iron regulatory protein 1
IRP1
Iron-responsive element-binding protein 1
IRE-BP 1
Gene Name: ACO1 |
| UniProt ID | P21399 (ACOC_HUMAN), Reviewed |
| GO terms | GO:0006099 tricarboxylic acid cycle
GO:0006101 citrate metabolic process
GO:0006417 regulation of translation
GO:0006879 cellular iron ion homeostasis
GO:0008152 metabolic process
GO:0009791 post-embryonic development
GO:0010040 response to iron(II) ion
GO:0010468 regulation of gene expression
GO:0050892 intestinal absorption
GO:0003723 RNA binding
GO:0003994 aconitate hydratase activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0030350 iron-responsive element binding
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005783 endoplasmic reticulum
GO:0005794 Golgi apparatus
GO:0005829 cytosol
GO:0070062 extracellular vesicular exosome
|
| Organisms for which functions have been demonstrated | Homo sapiens (human, a mammal) |
| Sequence length | 889 |
| FASTA sequence | >sp|P21399|ACOC_HUMAN Cytoplasmic aconitate hydratase OS=Homo sapiens GN=ACO1 PE=1 SV=3
MSNPFAHLAEPLDPVQPGKKFFNLNKLEDSRYGRLPFSIRVLLEAAIRNCDEFLVKKQDIENILHWNVTQHKNIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFHNMRIIPPGSGIIHQVNLEYLARVVFDQDGYYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYLVQTGRDEEKLKYIKKYLQAVGMFRDFNDPSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGFKGFQVAPEHHNDHKTFIYDNTEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGVVTYYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTIRIDFEKEPLGVNAKGQQVFLKDIWPTRDEIQAVERQYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKSTYIKSPPFFENLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVMARGTFANIRLLNRFLNKQAPQTIHLPSGEILDVFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGENADALGLTGQERYTIIIPENLKPQMKVQVKLDTGKTFQAVMRFDTDVELTYFLNGGILNYMIRKMAK
|
| Structure Information |
| PDB ID | 2B3X |
| Quaternary structure | |
| SCOP | The "swivelling" beta/beta/alpha domain, Aconitase iron-sulfur domain |
| CATH | 3.30.499.10, 3.40.1060.10, 6.10.190.10, 3.20.19.10 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-15, 395-413, 685-687, 888-889 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | aconitase, enzyme
4Fe-4S cluster in active site when cellular iron levels are high Citrate <=> isocitrate
Citric acid cycle |
| References for function | Philpott CC, Klausner RD, Rouault TA. The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation. Proc Natl Acad Sci U S A. 1994 Jul 19. PMID: 8041788 |
| E.C. number | 4.2.1.3 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | iron responsive element binding protein
when cellular iron concentrations are low, loses 4Fe-4S cluster and binds to iron-responsive elements (IRES) in mRNA that encodes proteins that are involved in iron uptake and use |
| References for function | Philpott CC, Klausner RD, Rouault TA. The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation. Proc Natl Acad Sci U S A. 1994 Jul 19. PMID: 8041788 |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |