A5ITM4
Gene name |
accD |
Protein name |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta |
Names |
ACCase subunit beta, Acetyl-CoA carboxylase carboxyltransferase subunit beta |
Species |
Staphylococcus aureus (strain JH9) |
KEGG Pathway |
saj:SaurJH9_1757 |
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 A5ITM4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A5ITM4-F1 | Predicted | AlphaFoldDB |
No variants for A5ITM4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A5ITM4 | |||||
No associated diseases with A5ITM4
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 |
| MFKDFFNRTK | KKKYLTVQDS | KNNDVPAGIM | TKCPKCKKIM | YTKELAENLN | VCFNCDHHIA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LTAYKRIEAI | SDEGSFTEFD | KGMTSANPLD | FPSYLEKIEK | DQQKTGLKEA | VVTGTAQLDG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MKFGVAVMDS | RFRMGSMGSV | IGEKICRIID | YCTENRLPFI | LFSASGGARM | QEGIISLMQM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GKTSVSLKRH | SDAGLLYISY | LTHPTTGGVS | ASFASVGDIN | LSEPKALIGF | AGRRVIEQTI |
| 250 | 260 | 270 | 280 | ||
| NEKLPDDFQT | AEFLLEHGQL | DKVVHRNDMR | QTLSEILKIH | QEVTK |