Reviewed,
UniProtKB/Swiss-Prot P58839 (G3P_METKA)
Last modified
June 16, 2009.
Version 54.
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 | Methanopyrus kandleri [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 2320 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus |
Protein attributes
| Sequence length | 350 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 – 350 | 350 | Glyceraldehyde-3-phosphate dehydrogenase HAMAP MF_00559 | PRO_0000145724 | |||||
Regions | |||||||||
| Nucleotide binding | 13 – 14 | 2 | NAD By similarity | ||||||
| Region | 147 – 149 | 3 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
| Region | 202 – 203 | 2 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
Sites | |||||||||
| Active site | 148 | 1 | Nucleophile By similarity | ||||||
| Binding site | 118 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 176 | 1 | NAD By similarity | ||||||
| Binding site | 309 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens." Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A. Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938. |
Cross-references
Sequence databases | |
|---|---|
| AE010355 Genomic DNA. Translation: AAM01833.1. | |
| RefSeq | NP_613903.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CF2 based on UniProtKB P10618. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1476719. |
| GenomeReviews | Gene locus MK0618 in contig AE009439_GR. |
| KEGG | mka:MK0618. |
| NMPDR | fig|190192.1.peg.616. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P58839. |
| OMA | P58839. AIFQGGE. |
Enzyme and pathway databases | |
| BioCyc | MKAN190192:MK0618-MON. |
| BRENDA | 1.2.1.59. 7577. |
Family and domain databases | |
| HAMAP | MF_00559. [Tree] |
| InterPro | IPR000173. GlycerAld_3-P_DH. IPR006436. Glyceraldehyde-3-P_DH_2_arc. [Graphical view] |
| 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_METKA | ||||||||
| Accession | Primary (citable) accession number: P58839 | ||||||||
| 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


