P0A509 (BCCA_MYCBO) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 46.
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: Acetyl-/propionyl-coenzyme A carboxylase alpha chain Including the following 2 domains:
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| Gene names |
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| Organism | Mycobacterium bovis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1765 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 654 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | This protein carries two functions: biotin carboxyl carrier protein and biotin carboxyltransferase By similarity. |
| Catalytic activity | ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]. |
| Cofactor | Biotin. |
| Pathway | |
| Subunit structure | Multimer comprised of 2 different subunits, the larger one (63/64 kDa) has biotin carboxylase and biotin carrier functions, while the smaller subunit possesses carboxyltransferase and substrate binding activity By similarity. |
| Sequence similarities | Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Ligand | ATP-binding Biotin Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome Multifunctional enzyme |
| 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 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 – 654 | 654 | Acetyl-/propionyl-coenzyme A carboxylase alpha chain | PRO_0000146796 | |||||
Regions | |||||||||
| Domain | 1 – 448 | 448 | Biotin carboxylation | ||||||
| Domain | 120 – 319 | 200 | ATP-grasp | ||||||
| Domain | 586 – 652 | 67 | Biotinyl-binding | ||||||
Sites | |||||||||
| Active site | 294 | 1 | By similarity | ||||||
| Binding site | 116 | 1 | ATP By similarity | ||||||
| Binding site | 200 | 1 | ATP By similarity | ||||||
| Binding site | 235 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 620 | 1 | N6-biotinyllysine By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. Hewinson R.G.Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX248342 Genomic DNA. Translation: CAD97390.1. |
| RefSeq | NP_856174.1. NC_002945.3. |
3D structure databases | |
| ProteinModelPortal | P0A509. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000017440; EBMYCP00000017275; EBMYCG00000017435. |
| GeneID | 1090579. |
| GenomeReviews | Gene locus Mb2529c in contig BX248333_GR. |
| KEGG | mbo:Mb2529c. |
| PATRIC | 18007289. VBIMycBov88188_2784. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000015717. |
| HOGENOM | HBG535236. |
| OMA | QVMGDKI. |
| ProtClustDB | CLSK791888. |
Enzyme and pathway databases | |
| BioCyc | MBOV233413:MB2529C-MONOMER. |
Family and domain databases | |
| InterPro | IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. 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. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR011054. Rudment_hybrid_motif. IPR011053. Single_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 | K11263. |
| Pfam | PF02785. Biotin_carb_C. 1 hit. PF00364. Biotin_lipoyl. 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 | SSF51230. Hybrid_motif. 1 hit. SSF52440. PreATP-grasp-like. 1 hit. SSF51246. Rudmnt_hyb_motif. 1 hit. |
| PROSITE | PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00188. BIOTIN. 1 hit. PS50968. BIOTINYL_LIPOYL. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BCCA_MYCBO | ||||||||
| Accession | Primary (citable) accession number: P0A509 Secondary accession number(s): P46401 | ||||||||
| 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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