Q01059
Gene name |
ACO1 (FRP, IREB1, IREBP) |
Protein name |
Cytoplasmic aconitate hydratase |
Names |
Aconitase, Citrate hydro-lyase, Ferritin repressor protein, Iron regulatory protein 1, IRP1, Iron-responsive element-binding protein 1, IRE-BP 1 |
Species |
Oryctolagus cuniculus (Rabbit) |
KEGG Pathway |
ocu:100009154 |
EC number |
4.2.1.3: Hydro-lyases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
3 structures for Q01059
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3SN2 | X-ray | 299 A | A | 2-889 | PDB |
| 3SNP | X-ray | 280 A | A/B | 2-889 | PDB |
| AF-Q01059-F1 | Predicted | AlphaFoldDB |
No variants for Q01059
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q01059 | |||||
No associated diseases with Q01059
5 regional properties for Q01059
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aconitase A/isopropylmalate dehydratase small subunit, swivel domain | 693 - 818 | IPR000573 |
| domain | Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha domain | 63 - 564 | IPR001030 |
| binding_site | Aconitase family, 4Fe-4S cluster binding site | 429 - 445 | IPR018136-1 |
| binding_site | Aconitase family, 4Fe-4S cluster binding site | 495 - 508 | IPR018136-2 |
| domain | Aconitase A, swivel domain | 670 - 839 | IPR044137 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.2.1.3 | Hydro-lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| aconitate hydratase activity | Catalysis of the reaction: citrate = isocitrate. The reaction occurs in two steps: (1) citrate = cis-aconitate + H2O, (2) cis-aconitate + H2O = isocitrate. This reaction is the interconversion of citrate and isocitrate via the labile, enzyme-bound intermediate cis-aconitate. Water is removed from one part of the citrate molecule and added back to a different atom to form isocitrate. |
| citrate dehydratase activity | Catalysis of the reaction: citrate = cis-aconitate + H2O. |
| iron-responsive element binding | Binding to an iron-responsive element, a regulatory sequence found in the 5'- and 3'-untranslated regions of mRNAs encoding many iron-binding proteins. |
| metal ion binding | Binding to a metal ion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular iron ion homeostasis | Any process involved in the maintenance of an internal steady state of iron ions at the level of a cell. |
| citrate metabolic process | The chemical reactions and pathways involving citrate, 2-hydroxy-1,2,3-propanetricarboyxlate. Citrate is widely distributed in nature and is an important intermediate in the TCA cycle and the glyoxylate cycle. |
| response to iron(II) ion | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an iron(II) ion stimulus. |
| tricarboxylic acid cycle | A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSNPFAYLAE | PLDPAQPGKK | FFNLNKLDYS | RYGRLPFSIR | VLLEAAVRNC | DKFLVKKEDI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ENILNWNVTQ | HMNIEVPFKP | ARVILQDFTG | VPSVVDFAAM | RDAVKKLGGD | PEKINPICPV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DLVIDHSIQV | DFNRRADSLQ | KNQDLEFERN | RERFEFLKWG | SKAFRNMRII | PPGSGIIHQV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NLEYLARVVF | DQDGYYYPDS | LVGTDSHTTM | IDGLGVLGWG | VGGIEAEAVM | LGQPISMVLP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QVIGYRLMGK | PHPLVTSTDI | VLTITKHLRQ | VGVVGKFVEF | FGLGVAQLSI | ADRATIANMC |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PEYGATATFF | PVDEVSIKYL | VQTGRDESKV | KQIRKYLQAV | GMFRDYSDPS | QDPDFTQVVE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LDLKTVVPCC | SGPKRPQDKV | AVSDMKKDFE | SCLGAKQGFK | GFQVAPDHHN | DHKTFIYNDS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EFTLSHGSVV | IAAITSCTNT | SNPSVMLGAG | LLAKKAVDAG | LNVKPYVKTS | LSPGSGVVTY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YLRESGVMPY | LSQLGFDVVG | YGCMTCIGNS | GPLPEPVVEA | ITQGDLVAVG | VLSGNRNFEG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RVHPNTRANY | LASPPLVIAY | AIAGTIRIDF | EKEPLGTNAK | GQQVFLRDIW | PTREEIQAVE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RQYVIPGMFT | EVYQKIETVN | ASWNALAAPS | DKLYLWNPKS | TYIKSPPFFE | NLTLDLQPPK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| SIVDAYVLLN | LGDSVTTDHI | SPAGNIARNS | PAARYLTNRG | LTPREFNSYG | SRRGNDAIMA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| RGTFANIRLL | NRFLNKQAPQ | TIHLPSGETL | DVFDAAERYQ | QEGHPLIVLA | GKEYGSGSSR |
| 790 | 800 | 810 | 820 | 830 | 840 |
| DWAAKGPFLL | GIKAVLAESY | ERIHRSNLVG | MGVIPLEYLP | GENADSLGLT | GRERYTIIIP |
| 850 | 860 | 870 | 880 | ||
| ENLTPRMHVQ | VKLDTGKTFQ | AVIRFDTDVE | LTYLHNGGIL | NYMIRKMAK |