Reviewed,
UniProtKB/Swiss-Prot P61879 (G3P_PYRFU)
Last modified
June 16, 2009.
Version 39.
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 furiosus [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 2261 [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 | Inferred from homology. |
General annotation (Comments)
| Function | Active in the presence of NAD and NADP By similarity. |
| 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 By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| 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: UniProtKB-SubCell |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADP or NADPH 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 HAMAP MF_00559 | PRO_0000145730 | |||||
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] | "The complete sequence of the Pyrococcus furiosus genome." Weiss R.B., Dunn D.M., Robb F.T., Brown J.R. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1. |
Cross-references
Sequence databases | |
|---|---|
| AE010282 Genomic DNA. Translation: AAL81998.1. | |
| RefSeq | NP_579603.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CF2 based on UniProtKB P10618. |
| SMR | P61879. Positions 1-334. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1469753. |
| GenomeReviews | Gene locus PF1874 in contig AE009950_GR. |
| KEGG | pfu:PF1874. |
| NMPDR | fig|186497.1.peg.1923. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P61879. |
| OMA | P61879. AIFQGGE. |
Enzyme and pathway databases | |
| BRENDA | 1.2.1.59. 321. |
Family and domain databases | |
| HAMAP | MF_00559. [Tree] |
| InterPro | IPR000173. GlycerAld_3-P_DH. IPR006436. Glyceraldehyde-3-P_DH_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_PYRFU | ||||||||
| Accession | Primary (citable) accession number: P61879 Secondary accession number(s): P20286 | ||||||||
| Entry history |
| ||||||||
| 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


