A4F5Q5
Gene name |
accD (accA, accDA, SACE_0026) |
Protein name |
Acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha |
Names |
ACCase subunits beta/alpha, Acetyl-CoA carboxylase carboxyltransferase subunits beta/alpha |
Species |
Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338) |
KEGG Pathway |
sen:SACE_0026 |
EC number |
2.1.3.15: Carboxy- and carbamoyltransferases |
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 A4F5Q5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A4F5Q5-F1 | Predicted | AlphaFoldDB |
No variants for A4F5Q5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A4F5Q5 | |||||
No associated diseases with A4F5Q5
4 regional properties for A4F5Q5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Acetyl-coenzyme A carboxyltransferase, N-terminal | 21 - 290 | IPR011762 |
| domain | Acetyl-coenzyme A carboxyltransferase, C-terminal | 286 - 536 | IPR011763 |
| domain | Acetyl-CoA carboxylase | 95 - 487 | IPR034733 |
| domain | Acetyl-coA carboxylase zinc finger domain | 22 - 47 | IPR041010 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.1.3.15 | Carboxy- and carbamoyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| acetyl-CoA carboxylase complex | A protein complex that catalyzes the first step in long-chain fatty acid biosynthesis. For example, in E. coli the complex is heterohexameric and composed of biotin carbonyl carrier protein, biotin carboxylase and the acetate CoA-transferase complex. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetyl-CoA carboxylase activity | Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| carboxyl- or carbamoyltransferase activity | Catalysis of the transfer of a carboxyl- or carbamoyl group from one compound (donor) to another (acceptor). |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid biosynthetic process | The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. |
| malonyl-CoA biosynthetic process | The chemical reactions and pathways resulting in the formation of malonyl-CoA, the S-malonyl derivative of coenzyme A. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAEPARTLAQ | DPRLADADQV | RWTRCPNCRS | LVYLRRLRRN | GHVCPDCAHH | MRMGVHDRIE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SLLDAGSFER | FGADVAPVDV | LGFTDSRPYT | ERLAQAQRRS | GSNEAVLCGT | GTIDGAPLVV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AALDFGFLGG | SVGGVTGELV | ARAARTALDR | RTPLVLVCAS | GGARMQEGTI | SLMQMAKTSQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EVARLHEAGV | LVVSIGTDPT | YGGVTASFGM | LGDVVVAEPG | ARIGFAGPQV | IRQTIRQELP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AGFQTAEYLR | DAGMVDLVVP | RHELRAHLAR | LLRVHSGGTA | APAAERGYRT | RPRPAADRDA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SEVLHAARDI | GRPSTSDYCA | RIFEDFVELH | GDRVSGDDPA | VVAGIGTLGG | RPVVVVGHQK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GHETAELVQR | NFGMPQPAGY | HKARRMMDYA | ERFGFPLVTF | VDTPGAHPGV | DAEQRGQGTA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IAECISRMAR | LKVPAVSVVT | GEGGSGGALA | LGVGNRVLVL | ENAYYSVISP | EGCSTILWGT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AERTSQAAEQ | LRITAEDLLR | LGVVDGVVDE | PAGGAQQDHA | AMASRLAAAL | RASIGELSEL |
| 550 | 560 | ||||
| DGDALLDQRR | RRFDRFGDPD | HSDSEVQP |