O06961 · TDCD_SALTY
- ProteinPropionate kinase
- GenetdcD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids402 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor.
Catalytic activity
- ATP + propanoate = ADP + propanoyl phosphate
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
112 μM | ATP | 7.5 | 25 | |||
2.3 mM | propionate | 7.5 | 25 | |||
26.9 mM | acetate | 7.5 | 25 |
Pathway
Amino-acid degradation; L-threonine degradation via propanoate pathway; propanoate from L-threonine: step 4/4.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 11 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 18 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 86 | substrate | ||||
Sequence: R | ||||||
Active site | 143 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 175 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 175 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 203-207 | ATP (UniProtKB | ChEBI) | ||||
Sequence: HLGNG | ||||||
Site | 236 | Transition state stabilizer | ||||
Sequence: R | ||||||
Binding site | 278-280 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DLR | ||||||
Binding site | 326-330 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GIGEN | ||||||
Binding site | 381 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | acetate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | propionate kinase activity | |
Biological Process | acetate metabolic process | |
Biological Process | L-threonine catabolic process to propionate |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePropionate kinase
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionO06961
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000107656 | 1-402 | Propionate kinase | |||
Sequence: MNEFPVVLVINCGSSSIKFSVLDVATCDVLMAGIADGMNTENAFLSINGDKPINLAHSNYEDALKAIAFELEKRDLTDSVALIGHRIAHGGELFTQSVIITDEIIDNIRRVSPLAPLHNYANLSGIDAARHLFPAVRQVAVFDTSFHQTLAPEAYLYGLPWEYFSSLGVRRYGFHGTSHRYVSRRAYELLDLDEKDSGLIVAHLGNGASICAVRNGQSVDTSMGMTPLEGLMMGTRSGDVDFGAMAWIAKETGQTLSDLERVVNKESGLLGISGLSSDLRVLEKAWHEGHERARLAIKTFVHRIARHIAGHAASLHRLDGIIFTGGIGENSVLIRQLVIEHLGVLGLTLDVEMNKQPNSHGERIISANPSQVICAVIPTNEEKMIALDAIHLGNVKAPVEFA |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length402
- Mass (Da)43,718
- Last updated2002-01-23 v2
- ChecksumEF387E43054FCAB3
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 135-142 | in Ref. 1; AAB53419 | ||||
Sequence: AVRQVAVF → GRASGGGI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U89718 EMBL· GenBank· DDBJ | AAB53419.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE006468 EMBL· GenBank· DDBJ | AAL22115.1 EMBL· GenBank· DDBJ | Genomic DNA |