A0A5B5VM95 · A0A5B5VM95_9BACT
- ProteinPyruvate, phosphate dikinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids909 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- ATP + phosphate + pyruvate = AMP + diphosphate + H+ + phosphoenolpyruvate
Cofactor
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 491 | Tele-phosphohistidine intermediate | ||||
Sequence: H | ||||||
Binding site | 597 | substrate | ||||
Sequence: R | ||||||
Binding site | 653 | substrate | ||||
Sequence: R | ||||||
Binding site | 780 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 780 | substrate | ||||
Sequence: E | ||||||
Binding site | 801 | substrate | ||||
Sequence: G | ||||||
Binding site | 802 | substrate | ||||
Sequence: T | ||||||
Binding site | 803 | substrate | ||||
Sequence: N | ||||||
Binding site | 804 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 804 | substrate | ||||
Sequence: D | ||||||
Active site | 866 | Proton donor | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | kinase activity | |
Molecular Function | metal ion binding | |
Molecular Function | pyruvate, phosphate dikinase activity | |
Biological Process | pyruvate metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate, phosphate dikinase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Rikenellaceae > Alistipes
Accessions
- Primary accessionA0A5B5VM95
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-391 | Pyruvate phosphate dikinase AMP/ATP-binding | ||||
Sequence: ELLGGKGANLAEMNLIGIPVPPGFTITTEVCAEYYAHGKEAVIKMLRPEVERAMQNIEKLTGMKFGDKEMPLLVSVRSGARASMPGMMDTILNLGMNDQAVEAVAKRTGNPRFAWDSYRRFVQMYGDVVLGMKPESKEDHDPFEVIIEEQKEKRGVKNDTDLTTDDLKELVQNFKAAVKKQTGEDFPACPWDQLWGAVCAVFGSWMNERAILYRKLNNIPAEWGTAVTVQAMVFGNMGANSATGVAFSRDAATGENLFNGEYLINAQGEDVVAGIRTPQQITIEGSKRWAVAQNVSEEERRTKYPSLEEVMPTVYKELDEIQRHLEQYFKDMQDIEFTIQDGKLWMLQCRNGKRTGAAMVKIAMDMLRE | ||||||
Domain | 459-539 | PEP-utilising enzyme mobile | ||||
Sequence: KAILVRIETSPEDLKGMLDAAGILTARGGMTSHAAVVARGMGKCCVSGAGELEIDYKTRTIRVNGFTVKEGDWISLNGSTG | ||||||
Domain | 555-904 | PEP-utilising enzyme C-terminal | ||||
Sequence: GDFGQLMELAGKYAVLKVRANADTPKDALQAFAFGAEGIGLCRTEHMFFEGDRIKAIREMILADDEAGRRVALAKLLPIQRGDFEGLFKAMNGFPVTVRLLDPPLHEFVPHDEKGQQEMAKEMNVPLQKIVAKVESLAEFNPMLGHRGCRLGNTYPEITEMQARAIIEAAMNVKAQGIPVHVEIMVPLVGNHKELRYQKGIIDATAEQVFSERNDKIDYMVGTMIEVPRAAVTANQIAEVAEFFSFGTNDLTQMTLGFSRDDIGKFLPVYLEKGILKNDPFQILDRNGVGQLIREAVFKGRSTREKLKCGICGEHGGEPSSVEFCHYAGLNYVSCSPFRVPIARLAAAHA |
Sequence similarities
Belongs to the PEP-utilizing enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length909
- Mass (Da)100,137
- Last updated2020-02-26 v1
- ChecksumD0EBBFCB3C845EF3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BQOL01000001 EMBL· GenBank· DDBJ | GKI18741.1 EMBL· GenBank· DDBJ | Genomic DNA |