K7GDN4 · K7GDN4_PELSI
- ProteinGlyceraldehyde-3-phosphate dehydrogenase
- GeneGAPDH
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids365 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC.
Catalytic activity
- D-glyceraldehyde 3-phosphate + phosphate + NAD+ = (2R)-3-phospho-glyceroyl phosphate + NADH + H+
- S-nitroso-L-cysteinyl-[GAPDH] + L-cysteinyl-[protein] = L-cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein]This reaction proceeds in the forward direction.
Pathway
Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 65 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 110 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 152 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 181-183 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SCT | ||||||
Active site | 182 | Nucleophile | ||||
Sequence: C | ||||||
Site | 209 | Activates thiol group during catalysis | ||||
Sequence: H | ||||||
Binding site | 212 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 241-242 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 264 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 346 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlyceraldehyde-3-phosphate dehydrogenase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Testudinata > Testudines > Cryptodira > Trionychia > Trionychidae > Pelodiscus
Accessions
- Primary accessionK7GDN4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-182 | Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding | ||||
Sequence: PRFGRIGRLVTRAAFTCDKVQIVAINDPFIDLNYMVSGTLVYNLEHSGCDKVQIVAINDPFIDLNYMVYMFKYDSTHGRFHGTVKAENGKLVINGQAITIFQERDPANIKWGDAGAEYVVESTGVFTTTEKASAHLKGGAKRVVISAPSADAPMFVMGVNHEKYDNSLKVVSNASC |
Sequence similarities
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length365
- Mass (Da)39,519
- Last updated2013-01-09 v1
- Checksum1E43FAA0E8887C18
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
K7GDM5 | K7GDM5_PELSI | GAPDH | 293 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGCU01093985 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |