P61879 (G3P_PYRFU) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 61.
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 |
| ||||||
| Organism | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) | ||||||
| Taxonomic identifier | 186497 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus |
Protein attributes
| Sequence length | 334 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Active in the presence of NAD and NADP By similarity. 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 By similarity. HAMAP MF_00559 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00559. |
| 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 Reference proteome |
| 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_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] | "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE009950 Genomic DNA. Translation: AAL81998.1. |
| RefSeq | NP_579603.1. NC_003413.1. |
3D structure databases | |
| ProteinModelPortal | P61879. |
| SMR | P61879. Positions 1-334. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBPYRT00000004606; EBPYRP00000004467; EBPYRG00000004606. |
| GeneID | 1469753. |
| GenomeReviews | Gene locus PF1874 in contig AE009950_GR. |
| KEGG | pfu:PF1874. |
| NMPDR | fig|186497.1.peg.1923. |
Phylogenomic databases | |
| GeneTree | EBGT00050000022490. |
| HOGENOM | HBG392099. |
| OMA | VPSHHGP. |
| ProtClustDB | PRK04207. |
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. |
| KO | K00150. |
| 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_PYRFU | ||||||||
| Accession | Primary (citable) accession number: P61879 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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