A0A5P2FWQ0 · A0A5P2FWQ0_9BACT
- ProteinAcetate kinase
- GeneackA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids394 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalytic activity
- acetate + ATP = acetyl phosphate + ADP
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Mg2+. Can also accept Mn2+.
Pathway
Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 12 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 19 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 94 | substrate | ||||
Sequence: R | ||||||
Active site | 150 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Site | 181 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 209-213 | ATP (UniProtKB | ChEBI) | ||||
Sequence: HLGNG | ||||||
Site | 242 | Transition state stabilizer | ||||
Sequence: R | ||||||
Binding site | 284-286 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DMR | ||||||
Binding site | 331-335 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GIGEN | ||||||
Binding site | 382 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | acetate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Biological Process | acetate metabolic process | |
Biological Process | acetyl-CoA biosynthetic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetate kinase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Chitinophagia > Chitinophagales > Chitinophagaceae > Rhizosphaericola
Accessions
- Primary accessionA0A5P2FWQ0
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length394
- Mass (Da)44,389
- Last updated2020-02-26 v1
- ChecksumE636092C7D31199F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP044016 EMBL· GenBank· DDBJ | QES87605.1 EMBL· GenBank· DDBJ | Genomic DNA |