P37251
Gene name |
ilvB (BSU28310) |
Protein name |
Acetolactate synthase large subunit |
Names |
AHAS, Acetohydroxy-acid synthase large subunit, ALS, Vegetative protein 105, VEG105 |
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU28310 |
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 P37251
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P37251-F1 | Predicted | AlphaFoldDB |
No variants for P37251
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P37251 | |||||
No associated diseases with P37251
4 regional properties for P37251
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Thiamine pyrophosphate enzyme, TPP-binding | 400 - 548 | IPR011766 |
| domain | Thiamine pyrophosphate enzyme, central domain | 207 - 342 | IPR012000 |
| domain | Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain | 18 - 180 | IPR012001 |
| domain | Acetolactate synthase large subunit, TPP binding domain | 378 - 563 | 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 |
|---|---|
| acetolactate synthase complex | A dimeric (a large and a small chain) or tetrameric (two large and two small chains) enzyme complex. Catalyzes the formation of acetolactate from pyruvate. |
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. |
2 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. |
| 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 |
| MGTNVQVDSA | SAECTQTMSG | ALMLIESLKK | EKVEMIFGYP | GGAVLPIYDK | LYNSGLVHIL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PRHEQGAIHA | AEGYARVSGK | PGVVIATSGP | GATNLVTGLA | DAMIDSLPLV | VFTGQVATSV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IGSDAFQEAD | ILGITMPVTK | HSYQVRQPED | LPRIIKEAFH | IATTGRPGPV | LIDIPKDVAT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IEGEFSYDHE | MNLPGYQPTT | EPNYLQIRKL | VEAVSSAKKP | VILAGAGVLH | GKASEELKNY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AEQQQIPVAH | TLLGLGGFPA | DHPLFLGMAG | MHGTYTANMA | LHECDLLISI | GARFDDRVTG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NLKHFARNAK | IAHIDIDPAE | IGKIMKTQIP | VVGDSKIVLQ | ELIKQDGKQS | DSSEWKKQLA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EWKEEYPLWY | VDNEEEGFKP | QKLIEYIHQF | TKGEAIVATD | VGQHQMWSAQ | FYPFQKADKW |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VTSGGLGTMG | FGLPAAIGAQ | LAEKDATVVA | VVGDGGFQMT | LQELDVIREL | NLPVKVVILN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NACLGMVRQW | QEIFYEERYS | ESKFASQPDF | VKLSEAYGIK | GIRISSEAEA | KEKLEEALTS |
| 550 | 560 | 570 | |||
| REPVVIDVRV | ASEEKVFPMV | APGKGLHEMV | GVKP |