A8BQ26 · A8BQ26_GIAIC
- ProteinPyruvate, phosphate dikinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids884 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- pyruvate + phosphate + ATP = phosphoenolpyruvate + AMP + diphosphate + H+
Cofactor
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 464 | Tele-phosphohistidine intermediate | ||||
Sequence: H | ||||||
Binding site | 570 | substrate | ||||
Sequence: R | ||||||
Binding site | 626 | substrate | ||||
Sequence: R | ||||||
Binding site | 753 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 753 | substrate | ||||
Sequence: E | ||||||
Binding site | 774 | substrate | ||||
Sequence: G | ||||||
Binding site | 775 | substrate | ||||
Sequence: T | ||||||
Binding site | 776 | substrate | ||||
Sequence: N | ||||||
Binding site | 777 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 777 | substrate | ||||
Sequence: D | ||||||
Active site | 839 | 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 | phosphorylation | |
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
Community suggested name: Gl-PPDK
Source | Submission date | Contributor |
---|---|---|
PubMed:25430456 | 0000-0002-6769-6896 |
Organism names
- Strain
- Taxonomic lineageEukaryota > Metamonada > Diplomonadida > Hexamitidae > Giardiinae > Giardia
Accessions
- Primary accessionA8BQ26
Proteomes
Organism-specific databases
Interaction
Protein-protein interaction databases
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 26-297 | Pyruvate phosphate dikinase AMP/ATP-binding | ||||
Sequence: VLGGKGISLAAMIKLGMPVPLGFTITCQTCVEYQKTASWPEGLKEEVASNLKLLEEKMGKTFGDNTNPLLVSVRSGAAVSMPGMMDTILNLGLNDESVKGLAAVTGNARFAYDSYRRFMQMFGDVCLGIDHDKFEHALDAVKTRYGRKTDPELTADELEEVCEAYRKICVAATGKTFPQCPHEQLELAINAVFRSWTNPRAQAYRTLNKLDHNMGTAVNVQSMVFGNTGDDSGTGVGFTRCPKTGEKFSYLYGEFLQNAQGEDVVAGIRTPV | ||||||
Domain | 313-367 | Pyruvate phosphate dikinase AMP/ATP-binding | ||||
Sequence: YDELSLIYAKLEGYYNDMVDLEFTVENGKLWMLQARAGKRTGFAMVRIAIDMCKE | ||||||
Domain | 431-512 | PEP-utilising enzyme mobile | ||||
Sequence: KKVILTRIETSPEDILGMDRAVGILTARGGQTSHAAVVARGMGKCCVAGADCCQINYATKTLVIGDRKFKEGDFISINGTTG | ||||||
Domain | 529-874 | PEP-utilising enzyme C-terminal | ||||
Sequence: DLQTIMDWSDKYRVLKIRTNADTPHDAAVARKFGAEGIGLCRTEHMFFAADRIMAMREMILSDDEGARRTALNKLLPFQREDFIGIFKAMDGKGVNIRLLDPPLHEFLPHTRDLQKKLAEDMNKKHRHIHERVEDLHEVNPMLGFRGVRLGIVYPEISEMQVRAILEAACIVSREGVTVKPEIMIPVLFSENEMEIMHALVNRVAASVFKEHGTTVDYEVGTMIELPRACVMADKIAQTAQYFSFGTNDLTQTTFGISRDDAGKFIPKYIDRGIFKVDPFVTLDQQGVGALMKMAIEGGRSTRTDMKIGICGEQTDPASILFLHKIGLNYVSCSPYRVPVARVAAA |
Sequence similarities
Belongs to the PEP-utilizing enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length884
- Mass (Da)97,659
- Last updated2007-11-13 v1
- ChecksumBB75BC63F088DFE4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AACB03000002 EMBL· GenBank· DDBJ | KAE8304094.1 EMBL· GenBank· DDBJ | Genomic DNA |