B1JDI2
Gene name |
leuA |
Protein name |
2-isopropylmalate synthase |
Names |
Alpha-IPM synthase, Alpha-isopropylmalate synthase |
Species |
Pseudomonas putida (strain W619) |
KEGG Pathway |
ppw:PputW619_4199 |
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
1 structures for B1JDI2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B1JDI2-F1 | Predicted | AlphaFoldDB |
No variants for B1JDI2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B1JDI2 | |||||
No associated diseases with B1JDI2
5 regional properties for B1JDI2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Pyruvate carboxyltransferase | 33 - 313 | IPR000891 |
| conserved_site | Alpha-isopropylmalate/homocitrate synthase, conserved site | 40 - 56 | IPR002034-1 |
| conserved_site | Alpha-isopropylmalate/homocitrate synthase, conserved site | 243 - 256 | IPR002034-2 |
| domain | 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain | 422 - 549 | IPR013709 |
| domain | LeuA, N-terminal catalytic TIM barrel domain | 32 - 315 | 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 | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
1 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(+). |
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 |
| MTMLKDPSKK | YRAFPTIELP | DRTWPSKTIT | EAPIWCSSDL | RDGNQSLIEP | MDSEKKLRFW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KTLVQVGVKE | IEASFPSASQ | TDFDFVRTLI | EDGHIPDDTT | IQVLTQARED | LIARTFESLR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GAKKAIVHLY | NATSPSFRRI | VFNQDKQGVK | DIAVNAAKLF | VKYAAQQPET | QWTFQYSPET |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FSATELEFAK | EVCDAVIEVW | NPTPEHKVIL | NLPATVEVAT | PNIYADQIEW | FCRNISRRDS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VIISLHCHND | RGTGIAATEL | GLMAGADRAE | GCLFGNGERT | GNVDLVTLAL | NLYTQGIDPQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LDFSDIDGVR | KVVEECNQLP | VHPRHPYVGD | LVHTAFSGSH | QDAIRKGFAK | QQDGELWEVP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YLPIDPADIG | RSYEAVIRVN | SQSGKGGITY | LLEQEYGISL | PRRMQIEFSQ | VVQGETDRLG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LEMTAQQIYS | LLHKEYLQAN | SPYALVSHRL | QEENGHSAVE | VEVAGEGETT | LHWRGKGNGA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LEALVAGLPI | AVEIMDYNEH | AIGAGTNAKA | AAYIELRVAG | GRPVHGVGID | ENITTASFKA |
| 550 | |||||
| LFSALNRSLS | QQEAKAA |