P9WQB3
Gene name |
leuA |
Protein name |
2-isopropylmalate synthase |
Names |
Alpha-IPM synthase, Alpha-isopropylmalate synthase |
Species |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
KEGG Pathway |
mtu:Rv3710 |
EC number |
2.3.3.13: Acyl groups converted into alkyl groups on transfer |
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
8 structures for P9WQB3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1SR9 | X-ray | 200 A | A/B | 1-644 | PDB |
| 3FIG | X-ray | 230 A | A/B | 3-644 | PDB |
| 3HPS | X-ray | 180 A | A/B | 1-644 | PDB |
| 3HPX | X-ray | 203 A | A/B | 1-425 | PDB |
| 3HPZ | X-ray | 220 A | A/B | 1-644 | PDB |
| 3HQ1 | X-ray | 170 A | A/B | 1-644 | PDB |
| 3U6W | X-ray | 221 A | A/B | 1-425 | PDB |
| AF-P9WQB3-F1 | Predicted | AlphaFoldDB |
No variants for P9WQB3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P9WQB3 | |||||
No associated diseases with P9WQB3
5 regional properties for P9WQB3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Pyruvate carboxyltransferase | 72 - 352 | IPR000891 |
| conserved_site | Alpha-isopropylmalate/homocitrate synthase, conserved site | 79 - 95 | IPR002034-1 |
| conserved_site | Alpha-isopropylmalate/homocitrate synthase, conserved site | 282 - 295 | IPR002034-2 |
| domain | 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain | 474 - 643 | IPR013709 |
| domain | LeuA, N-terminal catalytic TIM barrel domain | 71 - 354 | IPR039371 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.3.13 | Acyl groups converted into alkyl groups on transfer |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-isopropylmalate synthase activity | Catalysis of the reaction: 3-methyl-2-oxobutanoate + acetyl-CoA + H(2)O = (2S)-2-isopropylmalate + CoA + H(+). |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| manganese ion binding | Binding to a manganese ion (Mn). |
| potassium ion binding | Binding to a potassium ion (K+). |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| leucine biosynthetic process | The chemical reactions and pathways resulting in the formation of leucine, 2-amino-4-methylpentanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTTSESPDAY | TESFGAHTIV | KPAGPPRVGQ | PSWNPQRASS | MPVNRYRPFA | EEVEPIRLRN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RTWPDRVIDR | APLWCAVDLR | DGNQALIDPM | SPARKRRMFD | LLVRMGYKEI | EVGFPSASQT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DFDFVREIIE | QGAIPDDVTI | QVLTQCRPEL | IERTFQACSG | APRAIVHFYN | STSILQRRVV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FRANRAEVQA | IATDGARKCV | EQAAKYPGTQ | WRFEYSPESY | TGTELEYAKQ | VCDAVGEVIA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PTPERPIIFN | LPATVEMTTP | NVYADSIEWM | SRNLANRESV | ILSLHPHNDR | GTAVAAAELG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FAAGADRIEG | CLFGNGERTG | NVCLVTLGLN | LFSRGVDPQI | DFSNIDEIRR | TVEYCNQLPV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HERHPYGGDL | VYTAFSGSHQ | DAINKGLDAM | KLDADAADCD | VDDMLWQVPY | LPIDPRDVGR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TYEAVIRVNS | QSGKGGVAYI | MKTDHGLSLP | RRLQIEFSQV | IQKIAEGTAG | EGGEVSPKEM |
| 490 | 500 | 510 | 520 | 530 | 540 |
| WDAFAEEYLA | PVRPLERIRQ | HVDAADDDGG | TTSITATVKI | NGVETEISGS | GNGPLAAFVH |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ALADVGFDVA | VLDYYEHAMS | AGDDAQAAAY | VEASVTIASP | AQPGEAGRHA | SDPVTIASPA |
| 610 | 620 | 630 | 640 | ||
| QPGEAGRHAS | DPVTSKTVWG | VGIAPSITTA | SLRAVVSAVN | RAAR |