A0A2K2H9G3 · A0A2K2H9G3_9BACT
- ProteinPyruvate, phosphate dikinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids886 (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 | 466 | Tele-phosphohistidine intermediate | ||||
Sequence: H | ||||||
Binding site | 573 | substrate | ||||
Sequence: R | ||||||
Binding site | 629 | substrate | ||||
Sequence: R | ||||||
Binding site | 757 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 757 | substrate | ||||
Sequence: E | ||||||
Binding site | 778 | substrate | ||||
Sequence: G | ||||||
Binding site | 779 | substrate | ||||
Sequence: T | ||||||
Binding site | 780 | substrate | ||||
Sequence: N | ||||||
Binding site | 781 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 781 | substrate | ||||
Sequence: D | ||||||
Active site | 843 | 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 > Thermodesulfobacteriota > Desulfuromonadia > Desulfuromonadales > Geothermobacteraceae > Geothermobacter
Accessions
- Primary accessionA0A2K2H9G3
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-59 | Pyruvate phosphate dikinase AMP/ATP-binding | ||||
Sequence: NLLGGKGANLAEMTSIGLPVPAGFTLTTEVCTEFYKND | ||||||
Domain | 66-299 | Pyruvate phosphate dikinase AMP/ATP-binding | ||||
Sequence: LREEVARNLVKVEELMGKKFGDPSNPLLVSVRSGARASMPGMMDTVLNLGLNDETVKGIIAQSGDERFAYDSYRRFIQMYSNVVLGMDGDILEHLLGQMKEQRGVTLDTELTAVDLRELVSRFKTRVKEELGHDFPLDPQDQLWGAIGAVFGSWMNPRAITYRRLNNIPAEWGTAVTVQSMVFGNMGDDCATGVAFTRDPSTGEKIFYGEFLVNAQGEDVVAGIRTPQPINRDG | ||||||
Domain | 314-369 | Pyruvate phosphate dikinase AMP/ATP-binding | ||||
Sequence: CYAQLVKIKNILESHYRDMQDIEFTIEKHKLYMLQTRSGKRTAKAAVKIAVDMVRE | ||||||
Domain | 434-515 | PEP-utilising enzyme mobile | ||||
Sequence: KVILVRVETSPEDIHGMNAAQGILTARGGMTSHAAVVARGMGKCCVSGCGDIKVDYRAETLTTVSGLILKKGELITLDGSTG | ||||||
Domain | 530-880 | PEP-utilising enzyme C-terminal | ||||
Sequence: TGDFSQLMEWVDKARRLRVRTNADTPHDARVARAFGAEGIGLCRTEHMFFEAERIMAVREMILAADLDGRQRALEKIMPMQKGDFIGLFREMKGLPVTIRLLDPPLHEFLPQNDVEIEELAAEMRVPAATLKAKVESLHEFNPMLGHRGCRLAVTFPEIYDMQVRAIMEAACELIRNEGFSIVPEIMIPLVGEVRELAILRANVVRVADAVIAEYGVEVEYLIGTMIELPRAALTADVIAGEADFFSFGTNDLTQTTYGLSRDDSGRFLPFYIEQEIYATDPFVALDQEGVGQLVKMGCEKGRQARPDIKLGICGEHGGEPSSVIFCHNIGLDYVSCSPYRVPIARLAAAQ |
Sequence similarities
Belongs to the PEP-utilizing enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length886
- Mass (Da)97,229
- Last updated2018-03-28 v1
- Checksum08F43806623F664C