C1KVL9
Gene name |
accA |
Protein name |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
Names |
ACCase subunit alpha, Acetyl-CoA carboxylase carboxyltransferase subunit alpha |
Species |
Listeria monocytogenes serotype 4b (strain CLIP80459) |
KEGG Pathway |
lmc:Lm4b_01583 |
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 C1KVL9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C1KVL9-F1 | Predicted | AlphaFoldDB |
No variants for C1KVL9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C1KVL9 | |||||
No associated diseases with C1KVL9
1 regional properties for C1KVL9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Acetyl-coenzyme A carboxyltransferase, C-terminal | 38 - 292 | IPR011763 |
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. |
3 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). |
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 |
| MANEMEFEKP | ILELKSKIAD | LKEYNETSDV | DLTNEIEKLE | KRLAKLESSI | YSNMTAWDKF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QVARHPERPT | TLDYISLLFE | DFMELHGDRA | FGDDAAIVGG | IATFHGIPVT | VIGHQRGKDT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KDNLHRNFGM | PHPEGFRKAL | RLMKQADKFG | RPIICFIDTK | GAYPGRAAEE | RGQSEAIARN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LYEMSDMKVP | IISIVIGEGG | SGGALALGVG | NQIFMLENAV | FSVISPEGAA | AILWKDASQA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KKAAESMRIT | AGDLFELGIT | DGIIPEVKGG | AHRDLNAQAE | EINKTITKSL | HALMAFSEEQ |
| 310 | |||||
| LIEQRYEKFK | KIGVYDTL |