Reviewed,
UniProtKB/Swiss-Prot A4YHA5 (G3P_METS5)
Last modified
June 16, 2009.
Version 17.
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 | Metallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 399549 [NCBI] | ||||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Metallosphaera |
Protein attributes
| Sequence length | 340 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| 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 – 340 | 340 | Glyceraldehyde-3-phosphate dehydrogenase HAMAP MF_00559 | PRO_1000072562 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 12 | 2 | NAD By similarity | ||||||
| Region | 138 – 140 | 3 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
| Region | 193 – 194 | 2 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
Sites | |||||||||
| Active site | 139 | 1 | Nucleophile By similarity | ||||||
| Binding site | 109 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 167 | 1 | NAD By similarity | ||||||
| Binding site | 300 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | "Complete sequence of Metallosphaera sedula DSM 5348." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Han C., Detter J.C., Bruce D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. Richardson P.Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000682 Genomic DNA. Translation: ABP95807.1. | |
| RefSeq | YP_001191731.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5104857. |
| GenomeReviews | Gene locus Msed_1652 in contig CP000682_GR. |
| KEGG | mse:Msed_1652. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | A4YHA5. AIFQGGE. |
Family and domain databases | |
| HAMAP | MF_00559. [Tree] |
| InterPro | IPR000173. GlycerAld_3-P_DH. 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. |
| 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_METS5 | ||||||||
| Accession | Primary (citable) accession number: A4YHA5 | ||||||||
| 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


