Reviewed,
UniProtKB/Swiss-Prot P41911 (GPD2_YEAST)
Last modified
November 3, 2009.
Version 96.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial EC=1.1.1.8 | ||||||||
| 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 | 440 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)
| Function | Catalyzes the production of glycerol under anaerobic growth conditions. Glycerol production serves as a redox sink by consuming the excess cytosolic NADH during anaerobic metabolism. Ref.5 |
| Catalytic activity | sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH. |
| Subcellular location | |
| Induction | By anaerobic growth conditions and other conditions leading to accumulation of cytosolic NADH. Ref.11 Ref.6 |
| Miscellaneous | Present with 8966 molecules/cell in log phase SD medium. Ref.9 |
| Sequence similarities | Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. |
| Caution | It is uncertain whether Met-1 or Met-49 is the initiator. |
| Sequence caution | The sequence CAA84532.1 differs from that shown. Reason: Frameshift at position 411. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | NADH oxidation Ref.6 Inferred from mutant phenotype. Source: SGD glycerol-3-phosphate catabolic processInferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytosol Traceable author statement. Source: SGD glycerol-3-phosphate dehydrogenase complexInferred from electronic annotation. Source: InterPro mitochondrion Ref.10Inferred from direct assay. Source: SGD |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase (NAD+) activity Ref.6Inferred from mutant phenotype. Source: SGD protein homodimerization activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| IPP1 | P00817 | 1 | EBI-7791,EBI-9338 | |
| RNR1 | P21524 | 1 | EBI-7791,EBI-15234 | |
| RNR2 | P09938 | 1 | EBI-7791,EBI-15240 | |
| VMA2 | P16140 | 1 | EBI-7791,EBI-20254 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 16 | 16 | Mitochondrion Potential | ||||||
| Chain | 17 – 440 | 424 | Glycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial | PRO_0000043410 | |||||
Regions | |||||||||
| Nucleotide binding | 90 – 95 | 6 | NAD By similarity | ||||||
| Region | 359 – 360 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 294 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 178 | 1 | NAD By similarity | ||||||
| Binding site | 201 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 201 | 1 | Substrate By similarity | ||||||
| Binding site | 234 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 359 | 1 | NAD By similarity | ||||||
| Binding site | 388 | 1 | NAD By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 70 | 1 | Phosphoserine Ref.13 Ref.15 | ||||||
| Modified residue | 72 | 1 | Phosphoserine Ref.13 Ref.15 Ref.7 Ref.12 Ref.14 | ||||||
| Modified residue | 75 | 1 | Phosphoserine Ref.13 Ref.15 Ref.7 Ref.12 Ref.14 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of GPD2, a second gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) in Saccharomyces cerevisiae, and its comparison with GPD1." Eriksson P., Andre L., Ansell R., Blomberg A., Adler L. Mol. Microbiol. 17:95-107(1995) [PubMed: 7476212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Analysis of a 26 kb region on the left arm of yeast chromosome XV." Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H. Yeast 12:67-76(1996) [PubMed: 8789261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 90843 / S288c / FY73. |
| [3] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. Kleine K.Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 90843 / S288c / FY73. |
| [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: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [5] | "Physiological response to anaerobicity of glycerol-3-phosphate dehydrogenase mutants of Saccharomyces cerevisiae." Bjoerkqvist S., Ansell R., Adler L., Liden G. Appl. Environ. Microbiol. 63:128-132(1997) [PubMed: 8979347] [Abstract] Cited for: FUNCTION. |
| [6] | "The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation." Ansell R., Granath K., Hohmann S., Thevelein J.M., Adler L. EMBO J. 16:2179-2187(1997) [PubMed: 9171333] [Abstract] Cited for: INDUCTION. |
| [7] | "Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, MASS SPECTROMETRY. |
| [8] | "Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [9] | "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]. |
| [10] | "The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [11] | "Distinct intracellular localization of Gpd1p and Gpd2p, the two yeast isoforms of NAD+-dependent glycerol-3-phosphate dehydrogenase, explains their different contributions to redox-driven glycerol production." Valadi A., Granath K., Gustafsson L., Adler L. J. Biol. Chem. 279:39677-39685(2004) [PubMed: 15210723] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION. |
| [12] | "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, MASS SPECTROMETRY. |
| [13] | "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-70; SER-72 AND SER-75, MASS SPECTROMETRY. |
| [14] | "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, MASS SPECTROMETRY. |
| [15] | "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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-72 AND SER-75, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| Z35169 Genomic DNA. Translation: CAA84532.1. Sequence problems. X91067 Genomic DNA. Translation: CAA62526.1. Z74801 Genomic DNA. Translation: CAA99068.1. AY558560 Genomic DNA. Translation: AAS56886.1. | |
| PIR | S61719. |
| RefSeq | NP_014582.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:1348N. |
| IntAct | P41911. 12 interactions. |
| STRING | P41911. |
Proteomic databases | |
| PeptideAtlas | P41911. |
Genome annotation databases | |
| Ensembl | YOL059W; YOL059W; YOL059W; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 854095. |
| GenomeReviews | Gene locus YOL059W in contig Y13140_GR. |
| KEGG | sce:YOL059W. |
| NMPDR | fig|4932.3.peg.5674. |
Organism-specific databases | |
| CYGD | YOL059w. |
| SGD | S000005420. GPD2. |
Phylogenomic databases | |
| HOGENOM | P41911. |
| OMA | MEMVAFA. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.8. 250. |
Gene expression databases | |
| ArrayExpress | P41911. |
| Genevestigator | P41911. |
| GermOnline | YOL059W. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR013328. DH_multihelical. IPR016040. NAD(P)-bd_dom. IPR006168. NAD-dep_Gly3P_DH. IPR017751. NAD-dep_Gly3P_DH_euk. IPR011128. NAD-dep_Gly3P_DH_N. IPR006109. NAD_Gly3P_DH_C. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit. |
| PANTHER | PTHR11728. NAD_Gly3P_DH. 1 hit. |
| Pfam | PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. [Graphical view] |
| PRINTS | PR00077. GPDHDRGNASE. |
| ProDom | PD001278. NAD_Gly3P_C. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR03376. glycerol3P_DH. 1 hit. |
| PROSITE | PS00957. NAD_G3PDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 975758. |
Entry information
| Entry name | GPD2_YEAST | ||||||||
| Accession | Primary (citable) accession number: P41911 Secondary accession number(s): P50905 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


