A0A2S6WGM3 · A0A2S6WGM3_9ACTN
- ProteinPolyphosphate kinase
- Geneppk
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids774 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
Catalytic activity
- [phosphate](n) + ATP = [phosphate](n+1) + ADP
Cofactor
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 130 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 457 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 487 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 517 | Phosphohistidine intermediate | ||||
Sequence: H | ||||||
Binding site | 550 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 646 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 674 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | polyphosphate kinase complex | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | polyphosphate kinase activity | |
Biological Process | polyphosphate biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePolyphosphate kinase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A2S6WGM3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Post-translational modification
An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-53 | Disordered | ||||
Sequence: MKPTEPLPSGPSGPSDAPDSRAARKNGFMRQPNTQAEVQHTQPSVGSIAAHRP | ||||||
Compositional bias | 27-48 | Polar residues | ||||
Sequence: GFMRQPNTQAEVQHTQPSVGSI | ||||||
Domain | 92-198 | Polyphosphate kinase N-terminal | ||||
Sequence: FLDRERSWLAFNERVLELAEDPNTPLLERANFLAIFASNLDEFFMVRVAGLKRRIATGVATRSASGLQPREVLDMIWARSRELMARHAACFHEDVAPALAEEGIHLV | ||||||
Domain | 207-380 | Polyphosphate kinase middle | ||||
Sequence: EQARLFTLFRHRIFPVLTPLAVDPAHPFPYISGLSLNLAVVVRNPVTGHRHFARVKVPPLLSRFLEASPGRYVPVEDVIAAHLEELFPGMEVLEHHTFRLTRNEDLEVEEDDAENLLQALEKELMRRRLGPPVRLEVEESVDREVLDLLVRELKIGEAEVYPLPGPLDLTGLFR | ||||||
Domain | 412-578 | Polyphosphate kinase C-terminal | ||||
Sequence: DIFAALRTKDVLLHHPYDSFSTSVQAFLEQAATDPDVLAIKQTLYRTSGDSPIVDALIEAAESGKQVLVLVEIKARFDESANIKWARKLEEAGCHVVYGLVGLKTHCKLSLVVRQEGETLRRYSHVGTGNYHPKTARLYEDLGLLTSDPQVGADLSDLFNRLSGYSR | ||||||
Domain | 585-748 | Polyphosphate kinase C-terminal | ||||
Sequence: LLVAPKSLRDGLVSRIHKEIQHHRAGRPAHVRIKVNSMVDEAVIDACYRASQAGVPVDVWVRGICALRPGVPGLSENIRVRSVLGRFLEHSRVFAFGNGGEPEVWLGSADMMHRNLDRRIEALVRVTDPAHRAALNRLLDNGMSDTTASWHLGADGEWTRHATD |
Sequence similarities
Belongs to the polyphosphate kinase 1 (PPK1) family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length774
- Mass (Da)86,423
- Last updated2018-07-18 v1
- ChecksumB3364E1B600B80E1
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 27-48 | Polar residues | ||||
Sequence: GFMRQPNTQAEVQHTQPSVGSI |