Reviewed,
UniProtKB/Swiss-Prot P00358 (G3P2_YEAST)
Last modified
November 25, 2008.
Version 99.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glyceraldehyde-3-phosphate dehydrogenase 2 Short name=GAPDH 2 EC=1.2.1.12 | ||||||||
| Gene names |
| ||||||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 332 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Miscellaneous | There are three genes for G3PDH in yeast. Present with 121000 molecules/cell in log phase SD medium. |
| Sequence similarities | Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | apoptosis Inferred from mutant phenotype. Source: SGD gluconeogenesisInferred from expression pattern. Source: SGD glycolysisInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW oxygen and reactive oxygen species metabolic processInferred from mutant phenotype. Source: SGD |
| Cellular component | fungal-type cell wall Inferred from direct assay. Source: SGD lipid particleInferred from direct assay. Source: SGD mitochondrionInferred from direct assay. Source: SGD |
| Molecular function | NAD binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 332 | 331 | Glyceraldehyde-3-phosphate dehydrogenase 2 | PRO_0000145590 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 12 | 2 | NAD By similarity | ||||||
| Region | 149 – 151 | 3 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
| Region | 209 – 210 | 2 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
Sites | |||||||||
| Active site | 150 | 1 | Nucleophile By similarity | ||||||
| Binding site | 33 | 1 | NAD By similarity | ||||||
| Binding site | 78 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 180 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 232 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 314 | 1 | NAD By similarity | ||||||
| Site | 177 | 1 | Activates thiol group during catalysis By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 49 | 1 | Phosphoserine | ||||||
| Modified residue | 50 | 1 | Phosphothreonine | ||||||
| Modified residue | 54 | 1 | Phosphotyrosine | ||||||
| Modified residue | 59 | 1 | Phosphoserine | ||||||
| Modified residue | 149 | 1 | Phosphoserine | ||||||
| Modified residue | 201 | 1 | Phosphoserine | ||||||
| Modified residue | 310 | 1 | Phosphoserine | ||||||
| Modified residue | 319 | 1 | Phosphoserine | ||||||
| Modified residue | 320 | 1 | Phosphothreonine | ||||||
Experimental info | |||||||||
| Sequence conflict | 77 | 1 | E → A AA sequence Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "TDH2 is linked to MET3 on chromosome X of Saccharomyces cerevisiae." Mountain H.A., Korch C. Yeast 7:873-880(1991) [PubMed: 1789010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [2] | "Structural comparison of two nontandemly repeated yeast glyceraldehyde-3-phosphate dehydrogenase genes." Holland J.P., Holland M.J. J. Biol. Chem. 255:2596-2605(1980) [PubMed: 6244283] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. Karpfinger-Hartl L.EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [4] | "Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides." Norbeck J., Blomberg A. Electrophoresis 16:149-156(1995) [PubMed: 7737086] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-37; 72-77; 81-86; 199-213; 226-232 AND 322-331. Strain: ATCC 38531 / Y41. |
| [5] | Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F. Submitted (FEB-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13. Strain: ATCC 26786 / X2180-1A. |
| [6] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [7] | "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-201, MASS SPECTROMETRY. |
| [8] | "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; THR-50; TYR-54; SER-59; SER-310; SER-319 AND THR-320, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X60157 Genomic DNA. Translation: CAA42725.1. V01301 Genomic DNA. Translation: CAA24608.1. Sequence problems. X87611 Genomic DNA. Translation: CAA60931.1. Z49509 Genomic DNA. Translation: CAA89531.1. | |
| PIR | DEBYG1. S57024. |
| RefSeq | NP_012542.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DC5 based on UniProtKB P06977. |
| SMR | P00358. Positions 1-330. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:1951N. |
| IntAct | P00358. |
2-D gel databases | |
| SWISS-2DPAGE | P00358. |
| COMPLUYEAST-2DPAGE | P00358. |
Proteomic databases | |
| PeptideAtlas | P00358. |
Genome annotation databases | |
| Ensembl | YJR009C. Saccharomyces cerevisiae. [Contig view] |
| GeneID | 853465. |
| GenomeReviews | Gene locus YJR009C in contig Y13136_GR. |
| KEGG | sce:YJR009C. |
| NMPDR | fig|4932.3.peg.3516. |
Organism-specific databases | |
| CYGD | YJR009c. |
| SGD | S000003769. TDH2. |
| Yeast-GFP | Search... |
Phylogenomic databases | |
| HOGENOM | P00358. |
Gene expression databases | |
| ArrayExpress | P00358. |
| GermOnline | YJR009C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR000173. GlycerAld_3-P_DHase. IPR006424. Glyceraldehyde-3-P_DHase_1. [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. |
| PRINTS | PR00078. G3PDHDRGNASE. |
| TIGRFAMs | TIGR01534. GAPDH-I. 1 hit. |
| PROSITE | PS00071. GAPDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| LinkHub | P00358. |
| NextBio | 974053. |
Entry information
| Entry name | G3P2_YEAST | ||||||||
| Accession | Primary (citable) accession number: P00358 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome X Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names |

Clusters with


