Reviewed,
UniProtKB/Swiss-Prot P84546 (ACCC_POPEU)
Last modified
February 9, 2010.
Version 25.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Biotin carboxylase EC=6.3.4.14 Alternative name(s): Acetyl-CoA carboxylase subunit A Short name=ACC EC=6.4.1.2 |
| Organism | Populus euphratica (Euphrates poplar) |
| Taxonomic identifier | 75702 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Salicaceae › Saliceae › Populus |
Protein attributes
| Sequence length | 40 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA By similarity. UniProtKB Q06862 |
| Catalytic activity | ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein. UniProtKB Q06862 ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. |
| Pathway | Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. |
| Subunit structure | Acetyl-CoA carboxylase is an heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex By similarity. UniProtKB Q06862 |
| Sequence similarities | Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Ligand | ATP-binding Biotin Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activityInferred from electronic annotation. Source: EC biotin carboxylase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›40 | ›40 | Biotin carboxylase | PRO_0000146795 | |||||
Regions | |||||||||
| Domain | ‹1 – ›40 | ›40 | Biotin carboxylation | ||||||
| Domain | ‹13 – ›27 | ›15 | ATP-grasp | ||||||
Experimental info | |||||||||
| Non-adjacent residues | 12 – 13 | 2 | |||||||
| Non-adjacent residues | 27 – 28 | 2 | |||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 40 | 1 | |||||||
Sequences
References
| [1] | "Proteome profiling of Populus euphratica Oliv. upon heat stress." Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S., Roepstorff P., Pais M.S. Ann. Bot. 98:361-377(2006) [PubMed: 16740589] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Leaf. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 6.3.4.14. 293088. 6.4.1.2. 293088. |
Family and domain databases | |
| PROSITE | PS50975. ATP_GRASP. Partial match. PS50979. BC. Partial match. PS00866. CPSASE_1. Partial match. PS00867. CPSASE_2. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACCC_POPEU | ||||||||
| Accession | Primary (citable) accession number: P84546 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


