Q9I2A8
Gene name |
atoB (PA2001) |
Protein name |
Acetyl-CoA acetyltransferase |
Names |
Acetoacetyl-CoA thiolase |
Species |
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
KEGG Pathway |
pae:PA2001 |
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
1 structures for Q9I2A8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9I2A8-F1 | Predicted | AlphaFoldDB |
No variants for Q9I2A8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9I2A8 | |||||
No associated diseases with Q9I2A8
5 regional properties for Q9I2A8
| 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 | 271 - 390 | 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 |
|---|---|
| fatty acid beta-oxidation | A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQDVVIVAAT | RTAVGSFQGS | LAGIPAPELG | AAVIRRLLEQ | TGLDAGQVDE | VILGQVLTAG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SGQNPARQAA | IKAGLPVGVP | AMTLNKVCGS | GLKALHLGAQ | AIRCGDAEVI | VAGGQENMSL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| APYVMPGART | GLRMGHAKLV | DSMIEDGLWD | AFNDYHMGIT | AENLAEKYGL | TREEQDAFAA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ASQQKAIAAI | EGGRFRDEIT | PIQVPQRKGE | PLGFDTDEQP | RAGTTVEALA | KLKPAFRKDG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SVTAGNASSL | NDGAAAVLLM | SAAKAKALGL | PVLARIASYA | SAGVDPAIMG | IGPVSATRRA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LDKAGWSLEQ | LDLIEANEAF | AAQSLAVGRE | LGWDAARVNV | NGGAIALGHP | IGASGCRVLV |
| 370 | 380 | 390 | |||
| TLLHEMIRRD | AKKGLATLCI | GGGQGVALTL | ARD |