P63433
Gene name |
acnA (citB, SAV1350) |
Protein name |
Aconitate hydratase A |
Names |
ACN, Aconitase, (2R,3S)-2-methylisocitrate dehydratase, (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase, Iron-responsive protein-like, IRP-like, Probable 2-methyl-cis-aconitate hydratase, RNA-binding protein |
Species |
Staphylococcus aureus (strain Mu50 / ATCC 700699) |
KEGG Pathway |
sav:SAV1350 |
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
1 structures for P63433
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P63433-F1 | Predicted | AlphaFoldDB |
No variants for P63433
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P63433 | |||||
No associated diseases with P63433
4 regional properties for P63433
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | AMP-dependent synthetase/ligase domain | 92 - 535 | IPR000873 |
| conserved_site | AMP-binding, conserved site | 267 - 278 | IPR020845 |
| domain | AMP-binding enzyme, C-terminal domain | 544 - 625 | IPR025110 |
| domain | Acetyl-coenzyme A synthetase, N-terminal domain | 32 - 87 | IPR032387 |
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 | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-methylisocitrate dehydratase activity | Catalysis of the reaction: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = cis-2-methylaconitate + H(2)O. |
| 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. |
| metal ion binding | Binding to a metal ion. |
| mRNA 3'-UTR binding | Binding to a 3' untranslated region of an mRNA molecule. |
| mRNA binding | Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| propionate metabolic process, methylcitrate cycle | The chemical reactions and pathways involving propionate that occur in the methylcitrate cycle. |
| 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 |
| MAANFKEQSK | KHFDLNGQSY | TYYDLKAVEE | QGITKVSNLP | YSIRVLLESL | LRQEDDFVIT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DDHIKALSQF | GKDGNEGEVP | FKPSRVILQD | FTGVPAVVDL | ASLRKAMDDV | GGDITKINPE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VPVDLVIDHS | VQVDSYANPE | ALERNMKLEF | ERNYERYQFL | NWATKAFDNY | NAVPPATGIV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HQVNLEYLAS | VVHVRDVDGE | KTAFPDTLVG | TDSHTTMING | IGVLGWGVGG | IEAEAGMLGQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PSYFPIPEVI | GVRLVNSLPQ | GATATDLALR | VTQELRKKGV | VGKFVEFFGP | GVQHLPLADR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ATIANMAPEY | GATCGFFPVD | DESLKYMKLT | GRSDEHIALV | KEYLKQNHMF | FDVEKEDPNY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TDVIELDLST | VEASLSGPKR | PQDLIFLSDM | KSSFENSVTA | PAGNQGHGLD | KSEFDKKAEI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NFKDGSKATM | KTGDIAIAAI | TSCTNTSNPY | VMLGAGLVAK | KAVEKGLKVP | EYVKTSLAPG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SKVVTGYLRD | AGLQPYLDDL | GFNLVGYGCT | TCIGNSGPLL | PEIEKAIADE | DLLVTSVLSG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| NRNFEGRIHP | LVKANYLASP | QLVVAYALAG | TVDIDLQNEP | IGKGNDGEDV | YLKDIWPSIK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EVSDTVDSVV | TPELFIEEYN | NVYNNNELWN | EIDVTDQPLY | DFDPNSTYIQ | NPSFFQGLSK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EPGTIVPLNG | LRVMGKFGDS | VTTDHISPAG | AIGKDTPAGK | YLQDHQVPIR | EFNSYGSRRG |
| 730 | 740 | 750 | 760 | 770 | 780 |
| NHEVMVRGTF | ANIRIKNQLA | PGTEGGFTTY | WPTNEVMPIF | DAAMKYKEDG | TGLVVLAGND |
| 790 | 800 | 810 | 820 | 830 | 840 |
| YGMGSSRDWA | AKGTNLLGVK | TVIAQSYERI | HRSNLVMMGV | LPLEFKKGES | ADSLGLDGTE |
| 850 | 860 | 870 | 880 | 890 | 900 |
| EISVNIDENV | QPHDYVKVTA | KKQDGDLVEF | DAMVRFDSLV | EMDYYRHGGI | LQMVLRNKLA |
| Q |