P27818
Gene name |
|
Protein name |
Acetolactate synthase 1, chloroplastic |
Names |
ALS I, Acetohydroxy-acid synthase I, Acetolactate synthase I |
Species |
Brassica napus (Rape) |
KEGG Pathway |
bna:106366634 |
EC number |
2.2.1.6: Transketolases and transaldolases |
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 P27818
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P27818-F1 | Predicted | AlphaFoldDB |
No variants for P27818
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P27818 | |||||
No associated diseases with P27818
5 regional properties for P27818
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | TPP-binding enzyme, conserved site | 506 - 525 | IPR000399 |
| domain | Thiamine pyrophosphate enzyme, TPP-binding | 469 - 624 | IPR011766 |
| domain | Thiamine pyrophosphate enzyme, central domain | 276 - 405 | IPR012000 |
| domain | Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain | 83 - 246 | IPR012001 |
| domain | Acetolactate synthase large subunit, TPP binding domain | 447 - 639 | IPR039368 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.2.1.6 | Transketolases and transaldolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| chloroplast | A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetolactate synthase activity | Catalysis of the reaction: 2 pyruvate = 2-acetolactate + CO2. |
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| thiamine pyrophosphate binding | Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| isoleucine biosynthetic process | The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid. |
| response to herbicide | 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 a herbicide stimulus. Herbicides are chemicals used to kill or control the growth of plants. |
| valine biosynthetic process | The chemical reactions and pathways resulting in the formation of valine, 2-amino-3-methylbutanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAATSSSPI | SLTAKPSSKS | PLPISRFSLP | FSLTPQKDSS | RLHRPLAISA | VLNSPVNVAP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PSPEKTDKNK | TFVSRYAPDE | PRKGADILVE | ALERQGVETV | FAYPGGASME | IHQALTRSST |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IRNVLPRHEQ | GGVFAAEGYA | RSSGKPGICI | ATSGPGATNL | VSGLADAMLD | SVPLVAITGQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VPRRMIGTDA | FQETPIVEVT | RSITKHNYLV | MDVDDIPRIV | QEAFFLATSG | RPGPVLVDVP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KDIQQQLAIP | NWDQPMRLPG | YMSRLPQPPE | VSQLGQIVRL | ISESKRPVLY | VGGGSLNSSE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ELGRFVELTG | IPVASTLMGL | GSYPCNDELS | LQMLGMHGTV | YANYAVEHSD | LLLAFGVRFD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DRVTGKLEAF | ASRAKIVHID | IDSAEIGKNK | TPHVSVCGDV | KLALQGMNKV | LENRAEELKL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DFGVWRSELS | EQKQKFPLSF | KTFGEAIPPQ | YAIQILDELT | EGKAIISTGV | GQHQMWAAQF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YKYRKPRQWL | SSSGLGAMGF | GLPAAIGASV | ANPDAIVVDI | DGDGSFIMNV | QELATIRVEN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LPVKILLLNN | QHLGMVMQWE | DRFYKANRAH | TYLGDPAREN | EIFPNMLQFA | GACGIPAARV |
| 610 | 620 | 630 | 640 | 650 | |
| TKKEELREAI | QTMLDTPGPY | LLDVICPHQE | HVLPMIPSGG | TFKDVITEGD | GRTKY |