Q5E924 · G3PP2_ARATH
- ProteinGlyceraldehyde-3-phosphate dehydrogenase GAPCP2, chloroplastic
- GeneGAPCP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids420 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Involved in plastidial glycolytic pathway and plays a specific role in glycolytic energy production in non-green plastids and chloroplasts. Essential for breakdown of starch to form sucrose for export to non-photosynthetic tissues, and to generate primary metabolites for anabolic pathways such as fatty acid and amino acid synthesis. Plays an important role in plant development by providing substrates for the phosphorylated pathway of serine biosynthesis in roots. Plays a crucial role in pollen development. Functionally redundant with GAPCP1.
Catalytic activity
- D-glyceraldehyde 3-phosphate + phosphate + NAD+ = (2R)-3-phospho-glyceroyl phosphate + NADH + H+
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 94-95 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: RI | ||||||
Binding site | 116 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 162 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 233-235 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SCT | ||||||
Active site | 234 | Nucleophile | ||||
Sequence: C | ||||||
Site | 261 | Activates thiol group during catalysis | ||||
Sequence: H | ||||||
Binding site | 264 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 293-294 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 316 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 398 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast stroma | |
Cellular Component | plastid | |
Molecular Function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | |
Molecular Function | NAD binding | |
Molecular Function | NADP binding | |
Biological Process | carbohydrate metabolic process | |
Biological Process | glucose metabolic process | |
Biological Process | glycolytic process | |
Biological Process | intracellular amino acid homeostasis | |
Biological Process | primary root development |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlyceraldehyde-3-phosphate dehydrogenase GAPCP2, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ5E924
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal growth conditions. Gapcp1 and gapcp2 double mutants have severe dwarf phenotypes with arrested root development and male sterility. Pollen grains show shrunken and collapsed forms and cannot germinate.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 27 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-66 | Chloroplast | ||||
Sequence: MALSSLLRSAATSAAAPRVELYPSSSYNHSQVTSSLGFSHSLTSSRFSGAAVSTGKYNAKRVQPIK | ||||||
Chain | PRO_0000422408 | 67-420 | Glyceraldehyde-3-phosphate dehydrogenase GAPCP2, chloroplastic | |||
Sequence: ATATEAPPAVHRSRSSGKTKVGINGFGRIGRLVLRIATFRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNYKGTINVIDDSTLEINGKQVKVVSKRDPAEIPWADLGAEYVVESSGVFTTVGQASSHLKGGAKKVIISAPSADAPMFVVGVNEKTYLPNMDIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKDASYEDVKAAIKFASEGPLRGILGYTEEDVVSNDFLGDSRSSIFDANAGIGLSKSFMKLVSWYDNEWGYSNRVLDLIEHMALVAASR |
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in shoot and root vasculature, leaf veins and vascular tissue of flowers and siliques.
Gene expression databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length420
- Mass (Da)44,846
- Last updated2005-03-15 v1
- ChecksumE9FF3D655F281B63
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 58 | in Ref. 3; AAO22684 | ||||
Sequence: N → S | ||||||
Sequence conflict | 336 | in Ref. 5; AAM67077 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC006341 EMBL· GenBank· DDBJ | AAD34682.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002684 EMBL· GenBank· DDBJ | AEE29433.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT002867 EMBL· GenBank· DDBJ | AAO22684.1 EMBL· GenBank· DDBJ | mRNA | ||
BT021096 EMBL· GenBank· DDBJ | AAX12866.1 EMBL· GenBank· DDBJ | mRNA | ||
AY088762 EMBL· GenBank· DDBJ | AAM67077.1 EMBL· GenBank· DDBJ | mRNA |