P00360 (G3P1_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 146.
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 1 Short name=GAPDH 1 EC=1.2.1.12 | ||||||||
| Gene names |
| ||||||||
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome] | ||||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › ![]() |
Protein attributes
| Sequence length | 332 AA. |
| Sequence status | Complete. |
| 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 120000 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | gluconeogenesis Inferred from expression pattern PubMed 3905788. Source: SGD glycolysisInferred from expression pattern PubMed 3905788. Source: SGD |
| Cellular_component | fungal-type cell wall Inferred from direct assay PubMed 11158358. Source: SGD lipid particleInferred from direct assay PubMed 10515935. Source: SGD mitochondrionInferred from direct assay PubMed 16962558. Source: SGD plasma membraneInferred from direct assay PubMed 16622836. Source: SGD |
| Molecular_function | NAD binding Inferred from electronic annotation. Source: InterPro NADP bindingInferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activityInferred from direct assay PubMed 3905788. Source: SGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 332 | 332 | Glyceraldehyde-3-phosphate dehydrogenase 1 | PRO_0000145589 | |||||
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 | 43 | 1 | Phosphotyrosine Ref.11 | ||||||
| Modified residue | 124 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 125 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 149 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 182 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 199 | 1 | Phosphothreonine Ref.10 | ||||||
| Modified residue | 201 | 1 | Phosphoserine Ref.9 Ref.10 | ||||||
| Modified residue | 207 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 208 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 291 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 310 | 1 | Phosphoserine Ref.10 | ||||||
Experimental info | |||||||||
| Sequence conflict | 248 | 1 | E → A in CAA24609. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Homologous nucleotide sequences at the 5' termini of messenger RNAs synthesized from the yeast enolase and glyceraldehyde-3-phosphate dehydrogenase gene families. The primary structure of a third yeast glyceraldehyde-3-phosphate dehydrogenase gene." Holland J.P., Labieniec L., Swimmer C., Holland M.J. J. Biol. Chem. 258:5291-5299(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [3] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [4] | "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J.Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [5] | "Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins." Norbeck J., Blomberg A. Yeast 13:1519-1534(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 64-70 AND 218-225. Strain: ATCC 44827 / SKQ2N. |
| [6] | "Divergence of glyceraldehyde-3-phosphate dehydrogenase isozymes in Saccharomyces cerevisiae complex." Kadokura T., Ito T., Takano S., Nakazato A., Hara H., Watanabe S., Kudo T., Takeda M., Kaneko T. Syst. Appl. Microbiol. 23:198-205(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS. |
| [7] | "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M. Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [8] | "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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [9] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-201, MASS SPECTROMETRY. Strain: YAL6B. |
| [10] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-199; SER-201; SER-207; SER-208; SER-291 AND SER-310, MASS SPECTROMETRY. |
| [11] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43; SER-124; SER-125 AND THR-182, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | V01302 Genomic DNA. Translation: CAA24609.1. Z49327 Genomic DNA. Translation: CAA89343.1. AY693001 Genomic DNA. Translation: AAT93020.1. BK006943 Genomic DNA. Translation: DAA08747.1. |
| PIR | DEBYG3. S56824. |
| RefSeq | NP_012483.3. NM_001181485.3. |
3D structure databases | |
| ProteinModelPortal | P00360. |
| SMR | P00360. Positions 1-332. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-4304N. |
| IntAct | P00360. 20 interactions. |
| MINT | MINT-491516. |
| STRING | 4932.YJL052W. |
2D gel databases | |
| SWISS-2DPAGE | P00360. |
Proteomic databases | |
| PaxDb | P00360. |
| PeptideAtlas | P00360. |
| PRIDE | P00360. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | YJL052W; YJL052W; YJL052W. |
| GeneID | 853395. |
| KEGG | sce:YJL049W. sce:YJL052W. |
Organism-specific databases | |
| SGD | S000003588. TDH1. |
Phylogenomic databases | |
| eggNOG | COG0057. |
| GeneTree | ENSGT00690000101860. |
| HOGENOM | HOG000071678. |
| KO | K00134. K15053. |
| OMA | CHAYTAT. |
| OrthoDB | EOG4578GC. |
Enzyme and pathway databases | |
| SABIO-RK | P00360. |
| UniPathway | UPA00109; UER00184. |
Gene expression databases | |
| Genevestigator | P00360. |
| GermOnline | YJL052W. Saccharomyces cerevisiae. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| 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. IPR006424. Glyceraldehyde-3-P_DH_1. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR10836. PTHR10836. 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. |
| SMART | SM00846. Gp_dh_N. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01534. GAPDH-I. 1 hit. |
| PROSITE | PS00071. GAPDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 973876. |
Entry information
| Entry name | G3P1_YEAST | ||||||||
| Accession | Primary (citable) accession number: P00360 Secondary accession number(s): D6VWD1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome X Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
