Q8RWV0 · TKTC1_ARATH
- ProteinTransketolase-1, chloroplastic
- GeneTKL-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids741 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the reversible transfer of a two-carbon ketol group from fructose-6-phosphate or sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-4-phosphate or ribose-5-phosphate, respectively (By similarity).
Could act as a stress sensor involved in adaptation process
Could act as a stress sensor involved in adaptation process
Catalytic activity
- D-sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Cofactor
Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
Note: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.
Note: Binds 1 thiamine pyrophosphate per subunit.
Pathway
Carbohydrate biosynthesis; Calvin cycle.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 103 | substrate | ||||
Sequence: H | ||||||
Site | 103 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 143 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 192-194 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GPL | ||||||
Binding site | 233 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 234 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 263 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 263 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 265 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 340 | substrate | ||||
Sequence: H | ||||||
Binding site | 340 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 340 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 434 | substrate | ||||
Sequence: R | ||||||
Binding site | 461 | substrate | ||||
Sequence: S | ||||||
Active site | 488 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 488 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 515 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 539 | substrate | ||||
Sequence: H | ||||||
Binding site | 547 | substrate | ||||
Sequence: D | ||||||
Binding site | 598 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast envelope | |
Cellular Component | chloroplast stroma | |
Cellular Component | cytosol | |
Cellular Component | plastid | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA binding | |
Molecular Function | transketolase activity | |
Biological Process | reductive pentose-phosphate cycle |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTransketolase-1, chloroplastic
- EC number
- Short namesTK
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8RWV0
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-66 | Chloroplast | ||||
Sequence: MASTSSLALSQALLARAISHHGSDQRGSLPAFSGLKSTGSRASASSRRRIAQSMTKNRSLRPLVRA | ||||||
Modified residue | 67 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000421817 | 67-741 | Transketolase-1, chloroplastic | |||
Sequence: AAVETVEPTTDSSIVDKSVNSIRFLAIDAVEKAKSGHPGLPMGCAPMAHILYDEVMRYNPKNPYWFNRDRFVLSAGHGCMLLYALLHLAGYDSVQEEDLKQFRQWGSKTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDAEVVDHYTYAILGDGCQMEGISNEACSLAGHWGLGKLIAFYDDNHISIDGDTEIAFTENVDQRFEALGWHVIWVKNGNTGYDEIRAAIKEAKTVTDKPTLIKVTTTIGYGSPNKANSYSVHGAALGEKEVEATRNNLGWPYEPFQVPDDVKSHWSRHTPEGATLESDWSAKFAAYEKKYPEEASELKSIITGELPAGWEKALPTYTPESPGDATRNLSQQCLNALAKVVPGFLGGSADLASSNMTLLKAFGDFQKATPEERNLRFGVREHGMGAICNGIALHSPGLIPYCATFFVFTDYMRGAMRISALSEAGVIYVMTHDSIGLGEDGPTHQPIEHIASFRAMPNTLMFRPADGNETAGAYKIAVTKRKTPSILALSRQKLPHLPGTSIEGVEKGGYTISDDSSGNKPDVILIGTGSELEIAAQAAEVLRKDGKTVRVVSFVCWELFDEQSDEYKESVLPSDVSARVSIEAASTFGWGKIVGGKGKSIGINSFGASAPAPLLYKEFGITVEAVVDAAKSFF | ||||||
Modified residue | 428 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Up-regulated by salt, sorbitol, and abscisic acid (ABA).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 22-51 | Disordered | ||||
Sequence: GSDQRGSLPAFSGLKSTGSRASASSRRRIA | ||||||
Compositional bias | 30-51 | Polar residues | ||||
Sequence: PAFSGLKSTGSRASASSRRRIA |
Sequence similarities
Belongs to the transketolase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q8RWV0-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length741
- Mass (Da)79,968
- Last updated2002-06-01 v1
- Checksum5886543FBA70E79C
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4JBY2 | F4JBY2_ARATH | TKL1 | 740 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 30-51 | Polar residues | ||||
Sequence: PAFSGLKSTGSRASASSRRRIA | ||||||
Sequence conflict | 282 | in Ref. 4; AAM62766 | ||||
Sequence: R → L | ||||||
Sequence conflict | 482 | in Ref. 3; AAO29950 | ||||
Sequence: L → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL162295 EMBL· GenBank· DDBJ | CAB82679.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002686 EMBL· GenBank· DDBJ | AEE80103.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF424631 EMBL· GenBank· DDBJ | AAL11624.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AY091094 EMBL· GenBank· DDBJ | AAM14045.1 EMBL· GenBank· DDBJ | mRNA | ||
AY133860 EMBL· GenBank· DDBJ | AAM91794.1 EMBL· GenBank· DDBJ | mRNA | ||
BT000604 EMBL· GenBank· DDBJ | AAN18173.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
BT003331 EMBL· GenBank· DDBJ | AAO29950.1 EMBL· GenBank· DDBJ | mRNA | ||
AY085542 EMBL· GenBank· DDBJ | AAM62766.1 EMBL· GenBank· DDBJ | mRNA | ||
AK317159 EMBL· GenBank· DDBJ | BAH19845.1 EMBL· GenBank· DDBJ | mRNA |