C1F3B7 (C1F3B7_ACIC5) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 19.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Acetyl-coenzyme A synthetase HAMAP MF_01123 EC=6.2.1.1 HAMAP MF_01123 | ||||
| Gene names |
| ||||
| Organism | Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 240015 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Acidobacteria › Acidobacteriales › Acidobacteriaceae › Acidobacterium |
Protein attributes
| Sequence length | 653 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. HAMAP MF_01123 |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding HAMAP MF_01123 Nucleotide-binding |
| Molecular function | Ligase HAMAP MF_01123 EMBL ACO31372.1 |
| PTM | Acetylation HAMAP MF_01123 |
| 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: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 525 | 1 | By similarity HAMAP MF_01123 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 617 | 1 | N6-acetyllysine By similarity HAMAP MF_01123 | ||||||
Sequences
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References
| [1] | "Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. Kuske C.R.Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001472 Genomic DNA. Translation: ACO31372.1. |
| RefSeq | YP_002755829.1. NC_012483.1. |
3D structure databases | |
| ProteinModelPortal | C1F3B7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | C1F3B7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 7697956. |
| GenomeReviews | Gene locus ACP_2811 in contig CP001472_GR. |
| KEGG | aca:ACP_2811. |
| PATRIC | 20668861. VBIAciCap40988_2694. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | MISPRAS. |
| ProtClustDB | CLSK2467758. |
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 | C1F3B7_ACIC5 | ||||||||
| Accession | Primary (citable) accession number: C1F3B7 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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