C6KSV3 · C6KSV3_PLAF7
- Proteintransketolase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids672 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
- D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 31 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 71 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 119 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 121 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 160 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 160 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 161 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 190 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 190 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 192 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 266 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 266 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 441 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | transketolase activity | |
Biological Process | pentose-phosphate shunt |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nametransketolase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionC6KSV3
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 20 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 100 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 358-529 | Transketolase-like pyrimidine-binding | ||||
Sequence: GATRNLSGIVLNSINKIFPELIGGSADLSESNCTSLKEENDIKKNSYGNKYIRFGVREHGMVAITNGLYAYGGFKPYCGTFLNFYTYAFGALRLAALSNHHILCIATHDSVELGEDGPTHQPIEVLSLLRSTPNLNIIRPADGNEVSGAYLSHFSNPHTPTVIALCRNKVPH |
Sequence similarities
Belongs to the transketolase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length672
- Mass (Da)75,815
- Last updated2009-09-01 v1
- Checksum3BAC8A2EE068BCAA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL844505 EMBL· GenBank· DDBJ | CAG25349.1 EMBL· GenBank· DDBJ | Genomic DNA |