O52058 (ACCC_ALLVD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 69.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Biotin carboxylase EC=6.3.4.14 | ||||
| Gene names |
| ||||
| Organism | Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 572477 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Allochromatium |
Protein attributes
| Sequence length | 449 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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. |
| Catalytic activity | ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]. 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. |
| 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 | Complete proteome |
| 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 metal ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 449 | 449 | Biotin carboxylase | PRO_0000146790 | |||||
Regions | |||||||||
| Domain | 4 – 448 | 445 | Biotin carboxylation | ||||||
| Domain | 123 – 320 | 198 | ATP-grasp | ||||||
Sites | |||||||||
| Active site | 295 | 1 | Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 427 | 1 | I → L in AAB91545. Ref.2 | ||||||
| Sequence conflict | 437 | 1 | Missing in AAB91545. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete sequence of chromosome of Allochromatium vinosum DSM 180." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., Woyke T. Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17899 / DSM 180 / NBRC 103801 / D. |
| [2] | "Molecular genetic evidence for extracytoplasmic localization of sulfur globules in Chromatium vinosum." Pattaragulwanit K., Brune D.C., Trueper H.G., Dahl C. Arch. Microbiol. 169:434-444(1998) [PubMed: 9560425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 309-449. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001896 Genomic DNA. Translation: ADC62830.1. AF017119 Genomic DNA. Translation: AAB91545.1. |
| RefSeq | YP_003443862.1. NC_013851.1. |
3D structure databases | |
| ProteinModelPortal | O52058. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 8787270. |
| GenomeReviews | Gene locus Alvin_1906 in contig CP001896_GR. |
| KEGG | alv:Alvin_1906. |
| PATRIC | 31923588. VBIAllVin64954_1890. |
Organism-specific databases | |
| CMR | Search... |
Family and domain databases | |
| InterPro | IPR004549. Acetyl_CoA_COase_biotin_COase. IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR011054. Rudment_hybrid_motif. [Graphical view] |
| Gene3D | G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit. |
| KO | K01961. |
| Pfam | PF02785. Biotin_carb_C. 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] |
| SUPFAM | SSF52440. PreATP-grasp-like. 1 hit. SSF51246. Rudmnt_hyb_motif. 1 hit. |
| TIGRFAMs | TIGR00514. AccC. 1 hit. |
| PROSITE | PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACCC_ALLVD | ||||||||
| Accession | Primary (citable) accession number: O52058 Secondary accession number(s): D3RUH1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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