P14611
Gene name |
phaA |
Protein name |
Acetyl-CoA acetyltransferase |
Names |
Acetoacetyl-CoA thiolase, Beta-ketothiolase |
Species |
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) |
KEGG Pathway |
reh:H16_A1438 |
EC number |
2.3.1.9: Transferring groups other than amino-acyl groups |
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
4 structures for P14611
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4O99 | X-ray | 196 A | A/B/C/D | 2-393 | PDB |
| 4O9A | X-ray | 152 A | A/B/C/D | 2-393 | PDB |
| 4O9C | X-ray | 200 A | A/B/C/D/E/F/G/H | 1-393 | PDB |
| AF-P14611-F1 | Predicted | AlphaFoldDB |
No variants for P14611
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P14611 | |||||
No associated diseases with P14611
5 regional properties for P14611
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Thiolase, active site | 374 - 387 | IPR020610 |
| conserved_site | Thiolase, conserved site | 339 - 355 | IPR020613 |
| active_site | Thiolase, acyl-enzyme intermediate active site | 84 - 102 | IPR020615 |
| domain | Thiolase, N-terminal | 4 - 262 | IPR020616 |
| domain | Thiolase, C-terminal | 270 - 392 | IPR020617 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.9 | Transferring groups other than amino-acyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetyl-CoA C-acetyltransferase activity | Catalysis of the reaction: 2 acetyl-CoA = CoA + acetoacetyl-CoA. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| poly-hydroxybutyrate biosynthetic process | The chemical reactions and pathways resulting in the formation of poly-hydroxybutyrate (PHB), a polymer of beta-hydroxybutyrate and a common storage material of prokaryotic cells. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTDVVIVSAA | RTAVGKFGGS | LAKIPAPELG | AVVIKAALER | AGVKPEQVSE | VIMGQVLTAG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SGQNPARQAA | IKAGLPAMVP | AMTINKVCGS | GLKAVMLAAN | AIMAGDAEIV | VAGGQENMSA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| APHVLPGSRD | GFRMGDAKLV | DTMIVDGLWD | VYNQYHMGIT | AENVAKEYGI | TREAQDEFAV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GSQNKAEAAQ | KAGKFDEEIV | PVLIPQRKGD | PVAFKTDEFV | RQGATLDSMS | GLKPAFDKAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TVTAANASGL | NDGAAAVVVM | SAAKAKELGL | TPLATIKSYA | NAGVDPKVMG | MGPVPASKRA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSRAEWTPQD | LDLMEINEAF | AAQALAVHQQ | MGWDTSKVNV | NGGAIAIGHP | IGASGCRILV |
| 370 | 380 | 390 | |||
| TLLHEMKRRD | AKKGLASLCI | GGGMGVALAV | ERK |