Q6MNF1 (ACSA_BDEBA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 45.
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-coenzyme A synthetase EC=6.2.1.1 Alternative name(s): Acetate--CoA ligase Acyl-activating enzyme | ||||
| Gene names |
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| Organism | Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 264462 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Deltaproteobacteria › Bdellovibrionales › Bdellovibrionaceae › Bdellovibrio |
Protein attributes
| Sequence length | 645 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP MF_01123 |
| Post-translational modification | Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP MF_01123 |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Acetylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Molecular function | AMP binding Inferred from electronic annotation. Source: InterPro ATP bindingInferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase 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 – 645 | 645 | Acetyl-coenzyme A synthetase HAMAP MF_01123 | PRO_1000065272 | |||||
Sites | |||||||||
| Active site | 514 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 606 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective." Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C. Science 303:689-692(2004) [PubMed: 14752164] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842649 Genomic DNA. Translation: CAE79201.1. |
| RefSeq | NP_968208.1. NC_005363.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PG4 based on UniProtKB Q8ZKF6. |
| ProteinModelPortal | Q6MNF1. |
| SMR | Q6MNF1. Positions 2-642. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2734497. |
| GenomeReviews | Gene locus Bd1306 in contig BX842601_GR. |
| KEGG | bba:Bd1306. |
| NMPDR | fig|264462.1.peg.1178. |
| PATRIC | 21077202. VBIBdeBac73187_1181. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG547964. |
| OMA | KGKPYML. |
| PhylomeDB | Q6MNF1. |
Enzyme and pathway databases | |
| BioCyc | BBAC264462:BD1306-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01123. Ac_CoA_synth. [Tree] |
| InterPro | IPR011904. Ac_CoA_lig. IPR024597. Acyl-CoA_synth_DUF3448. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view] |
| KO | K01895. |
| PANTHER | PTHR24095:SF42. PTHR24095:SF42. 1 hit. |
| Pfam | PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02188. Ac_CoA_lig_AcsA. 1 hit. |
| PROSITE | PS00455. AMP_BINDING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACSA_BDEBA | ||||||||
| Accession | Primary (citable) accession number: Q6MNF1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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