Reviewed,
UniProtKB/Swiss-Prot P61880 (G3P_PYRWO)
Last modified
November 25, 2008.
Version 33.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glyceraldehyde-3-phosphate dehydrogenase Short name=GAPDH EC=1.2.1.59 Alternative name(s): NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase | ||||
| Gene names |
| ||||
| Organism | Pyrococcus woesei | ||||
| Taxonomic identifier | 2262 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus |
Protein attributes
| Sequence length | 334 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Active in the presence of NAD and NADP. |
| Catalytic activity | D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Sequence similarities | Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. |
| Biophysicochemical properties | Temperature dependence: Thermostable. Has a 44 minutes half-life at 100 degrees Celsius. |
Ontologies
Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: HAMAP |
| Molecular function | NAD binding Inferred from electronic annotation. Source: InterPro NADP bindingInferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activityInferred from electronic annotation. Source: EC glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 334 | 334 | Glyceraldehyde-3-phosphate dehydrogenase | PRO_0000145733 | |||||
Regions | |||||||||
| Nucleotide binding | 12 – 13 | 2 | NAD By similarity | ||||||
| Region | 140 – 142 | 3 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
| Region | 192 – 193 | 2 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
Sites | |||||||||
| Active site | 141 | 1 | Nucleophile By similarity | ||||||
| Binding site | 111 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 167 | 1 | NAD By similarity | ||||||
| Binding site | 298 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | "Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli." Zwickl P., Fabry S., Bogedain C., Haas A., Hensel R. J. Bacteriol. 172:4329-4338(1990) [PubMed: 2165475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, CHARACTERIZATION. Strain: DSM 3773. |
Cross-references
Sequence databases | |
|---|---|
| M83988 Genomic DNA. Translation: AAA73180.1. | |
| PIR | DEQYG. S10653. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CF2 based on UniProtKB P10618. |
| SMR | P61880. Positions 1-334. |
| ModBase | Search... |
Family and domain databases | |
| HAMAP | MF_00559. [Tree] |
| InterPro | IPR000173. GlycerAld_3-P_DHase. IPR006436. Glyceraldehyde-3-P_DHase_2_arc. [Graphical view] |
| PANTHER | PTHR10836. GAP_DH. 1 hit. |
| Pfam | PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000149. GAP_DH. 1 hit. |
| ProDom | PD007761. GAPDH_like. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01546. GAPDH-II_archae. 1 hit. |
| PROSITE | PS00071. GAPDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | G3P_PYRWO | ||||||||
| Accession | Primary (citable) accession number: P61880 Secondary accession number(s): P20286 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


