Reviewed,
UniProtKB/Swiss-Prot Q81KY9 (ACCA_BACAN)
Last modified
February 9, 2010.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha Short name=Acetyl-CoA carboxylase carboxyltransferase subunit alpha Short name=ACCase subunit alpha EC=6.4.1.2 | ||||
| Gene names |
| ||||
| Organism | Bacillus anthracis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 324 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA By similarity. HAMAP MF_00823 |
| Catalytic activity | ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP MF_00823 |
| Pathway | Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP MF_00823 |
| Subunit structure | Acetyl-CoA carboxylase is an heterohexamer composed of biotin carboxyl carrier protein (accB), biotin carboxylase (accC) and two subunits each of ACCase subunit alpha (accA) and ACCase subunit beta (accD) By similarity. HAMAP MF_00823 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00823. |
| Sequence similarities | Belongs to the accA family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 324 | 324 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823 | PRO_0000223727 | |||
Sequences
| ||||||||||||||||||
References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP28534.1. AE017334 Genomic DNA. Translation: AAT33964.1. AE017225 Genomic DNA. Translation: AAT56792.1. |
| RefSeq | NP_847048.1. YP_021489.1. YP_030742.1. |
3D structure databases | |
| SMR | Q81KY9. Positions 4-312. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1083998. 2814345. 2851550. |
| GenomeReviews | Gene locus BA_4845 in contig AE016879_GR. Gene locus BAS4494 in contig AE017225_GR. Gene locus GBAA_4845 in contig AE017334_GR. |
| KEGG | ban:BA4845. bar:GBAA4845. bat:BAS4494. |
| TIGR | BA_4845. GBAA_4845. |
Phylogenomic databases | |
| HOGENOM | HBG286557. |
| OMA | HSVYTVA. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS4494-MONOMER. BANT261594:GBAA4845-MONOMER. |
| BRENDA | 6.4.1.2. 267517. |
Family and domain databases | |
| HAMAP | MF_00823. AcetylCoA_CT_alpha. [Tree] |
| InterPro | IPR001095. Acetyl_CoA_COase_a_su. IPR020582. Acetyl_CoA_COase_a_su_cons-reg. IPR011763. COA_CT_C. [Graphical view] |
| PANTHER | PTHR22855:SF3. Ac-CoA_carboxylA. 1 hit. |
| Pfam | PF03255. ACCA. 1 hit. [Graphical view] |
| PRINTS | PR01069. ACCCTRFRASEA. |
| TIGRFAMs | TIGR00513. accA. 1 hit. |
| PROSITE | PS50989. COA_CT_CTER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACCA_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81KY9 Secondary accession number(s): Q6HSE6, Q6KLP1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


