Reviewed,
UniProtKB/Swiss-Prot P11029 (ACAC_CHICK)
Last modified
January 19, 2010.
Version 93.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Acetyl-CoA carboxylase Short name=ACC EC=6.4.1.2 Including the following 1 domains: 1- Recommended name: Biotin carboxylase EC=6.3.4.14 | ||
| Gene names |
| ||
| Organism | Gallus gallus (Chicken) | ||
| Taxonomic identifier | 9031 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus |
Protein attributes
| Sequence length | 2324 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. |
| Catalytic activity | ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein. |
| Cofactor | Biotin By similarity. Binds 2 manganese ions per subunit By similarity. |
| Enzyme regulation | By phosphorylation. |
| Pathway | Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. |
| Subcellular location | |
| Sequence similarities | Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. Contains 1 carboxyltransferase domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Biotin Manganese Metal-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Direct protein sequencing Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activityInferred from electronic annotation. Source: EC biotin bindingInferred from electronic annotation. Source: InterPro biotin carboxylase activityInferred from electronic annotation. Source: EC manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2324 | 2324 | Acetyl-CoA carboxylase | PRO_0000146768 | |||||
Regions | |||||||||
| Domain | 117 – 618 | 502 | Biotin carboxylation | ||||||
| Domain | 275 – 466 | 192 | ATP-grasp | ||||||
| Domain | 752 – 818 | 67 | Biotinyl-binding | ||||||
| Domain | 1675 – 2171 | 497 | Carboxyltransferase | ||||||
| Nucleotide binding | 315 – 320 | 6 | ATP Potential | ||||||
Sites | |||||||||
| Active site | 441 | 1 | By similarity | ||||||
| Metal binding | 424 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 437 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 437 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 439 | 1 | Manganese 2 By similarity | ||||||
| Binding site | 1800 | 1 | Coenzyme A By similarity | ||||||
| Binding site | 2104 | 1 | Coenzyme A By similarity | ||||||
| Binding site | 2106 | 1 | Coenzyme A By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.3 | ||||||
| Modified residue | 78 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 80 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 786 | 1 | N6-biotinyllysine | ||||||
| Modified residue | 1193 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Primary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence." Takai T., Yokoyama C., Wada K., Tanabe T. J. Biol. Chem. 263:2651-2657(1988) [PubMed: 2893793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Liver. |
| [2] | "Primary structure of the biotin-binding site of chicken liver acetyl-CoA carboxylase." Takai T., Wada K., Tanabe T. FEBS Lett. 212:98-102(1987) [PubMed: 2879745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 493-820. Tissue: Liver. |
| [3] | Bienvenut W.V., Black E.J., Gillespie D.A. Submitted (JAN-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-18; 99-111; 121-132; 153-163; 278-288; 300-311; 336-350; 589-607; 742-755; 826-845; 1083-1096; 1147-1155; 1157-1169; 1233-1239; 1275-1286; 1319-1326; 1349-1362; 1365-1377; 1387-1397; 1653-1678; 1701-1708; 1727-1737; 1759-1775; 1801-1810; 1815-1833; 1882-1891; 1899-1906; 1955-1986; 2040-2049; 2067-2080; 2092-2104; 2177-2186; 2190-2195; 2199-2206 AND 2209-2226, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: B-cell lymphoma. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | J03541 mRNA. Translation: AAA48701.1. X05019 mRNA. Translation: CAA28675.1. |
| IPI | IPI00583030. |
| PIR | A29924. |
| RefSeq | NP_990836.1. |
| UniGene | Gga.1480 |
3D structure databases | |
| SMR | P11029. Positions 97-616, 742-834, 1551-2285. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P11029. |
Proteomic databases | |
| PRIDE | P11029. |
Genome annotation databases | |
| GeneID | 396504. |
| KEGG | gga:396504. |
Organism-specific databases | |
| CTD | 396504. |
Phylogenomic databases | |
| HOVERGEN | P11029. |
| PhylomeDB | P11029. |
Enzyme and pathway databases | |
| BRENDA | 6.3.4.14. 4. 6.4.1.2. 4. |
Family and domain databases | |
| InterPro | IPR013537. AcCoA_COase_cen. IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR001882. Biotin_BS. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR000089. Biotin_lipoyl. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR000022. Carboxyl_trans. IPR011763. COA_CT_C. IPR011762. COA_CT_N. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR011054. Rudment_hybrid_motif. IPR011053. Single_hybrid_motif. [Graphical view] |
| Gene3D | G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit. |
| Pfam | PF08326. ACC_central. 1 hit. PF02785. Biotin_carb_C. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF01039. Carboxyl_trans. 1 hit. PF00289. CPSase_L_chain. 1 hit. PF02786. CPSase_L_D2. 1 hit. [Graphical view] |
| SMART | SM00878. Biotin_carb_C. 1 hit. [Graphical view] |
| PROSITE | PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00188. BIOTIN. 1 hit. PS50968. BIOTINYL_LIPOYL. 1 hit. PS50989. COA_CT_CTER. 1 hit. PS50980. COA_CT_NTER. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACAC_CHICK | ||||||||
| Accession | Primary (citable) accession number: P11029 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
