P61880 (G3P_PYRWO) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 28, 2011.
Version 52.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
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| Organism | Pyrococcus woesei | ||||
| Taxonomic identifier | 2262 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus |
Protein attributes
| Sequence length | 334 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Active in the presence of NAD and NADP. HAMAP MF_00559 |
| Catalytic activity | D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H. HAMAP MF_00559 |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. HAMAP MF_00559 |
| 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. HAMAP MF_00559 |
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: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 |
| 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 HAMAP MF_00559 | 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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M83988 Genomic DNA. Translation: AAA73180.1. |
| PIR | DEQYG. S10653. |
3D structure databases | |
| ProteinModelPortal | P61880. |
| SMR | P61880. Positions 1-334. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| HAMAP | MF_00559. G3P_dehdrog_arch. [Tree] |
| InterPro | IPR020831. GlycerAld/Erythrose_P_DH. IPR020830. GlycerAld_3-P_DH_AS. IPR020829. GlycerAld_3-P_DH_cat. IPR020828. GlycerAld_3-P_DH_NAD(P)-bd. IPR006436. Glyceraldehyde-3-P_DH_2_arc. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000149. GAP_DH. 1 hit. |
| SMART | SM00846. Gp_dh_N. 1 hit. [Graphical view] |
| 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 program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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