P41911 (GPD2_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 129.
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: Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, mitochondrial EC=1.1.1.8 | ||||||||
| Gene names |
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| 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 | 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.6 |
| 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.7 Ref.12 |
| Miscellaneous | Present with 8966 molecules/cell in log phase SD medium. |
| 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | NADH oxidation Inferred from mutant phenotype Ref.7. Source: SGD glycerol metabolic processInferred from mutant phenotype Ref.7. Source: SGD glycerol-3-phosphate catabolic processInferred from electronic annotation. Source: InterPro |
| Cellular_component | cytosol Traceable author statement PubMed 10781551. Source: SGD glycerol-3-phosphate dehydrogenase complexInferred from electronic annotation. Source: InterPro mitochondrionInferred from direct assay Ref.11PubMed 16823961PubMed 17054397. Source: SGD |
| Molecular_function | NAD binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase [NAD+] activityInferred from mutant phenotype Ref.7. Source: SGD |
| Complete GO annotation... | |
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.14 Ref.16 | ||||||
| Modified residue | 72 | 1 | Phosphoserine Ref.8 Ref.13 Ref.14 Ref.15 Ref.16 | ||||||
| Modified residue | 75 | 1 | Phosphoserine Ref.8 Ref.13 Ref.14 Ref.15 Ref.16 | ||||||
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 90843 / S288c / FY73. |
| [4] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [5] | "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. |
| [6] | "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] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [7] | "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] [Europe PMC] [Abstract] Cited for: INDUCTION. |
| [8] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, MASS SPECTROMETRY. Strain: 2124. |
| [9] | "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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [10] | "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]. |
| [11] | "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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499. |
| [12] | "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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION. |
| [13] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, MASS SPECTROMETRY. Strain: ADR376. |
| [14] | "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 SER-70; SER-72 AND SER-75, MASS SPECTROMETRY. |
| [15] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, MASS SPECTROMETRY. |
| [16] | "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 SER-70; SER-72 AND SER-75, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | 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. BK006948 Genomic DNA. Translation: DAA10724.1. |
| PIR | S61719. |
| RefSeq | NP_014582.1. NM_001183314.1. |
3D structure databases | |
| ProteinModelPortal | P41911. |
| SMR | P41911. Positions 83-434. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-1348N. |
| IntAct | P41911. 6 interactions. |
| MINT | MINT-411876. |
| STRING | 4932.YOL059W. |
Proteomic databases | |
| PaxDb | P41911. |
| PeptideAtlas | P41911. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | YOL059W; YOL059W; YOL059W. |
| GeneID | 854095. |
| KEGG | sce:YOL059W. |
Organism-specific databases | |
| CYGD | YOL059w. |
| SGD | S000005420. GPD2. |
Phylogenomic databases | |
| eggNOG | COG0240. |
| GeneTree | ENSGT00390000003114. |
| HOGENOM | HOG000246855. |
| KO | K00006. |
| OMA | AVHEIST. |
| OrthoDB | EOG4FBN2Q. |
Gene expression databases | |
| Genevestigator | P41911. |
| GermOnline | YOL059W. Saccharomyces cerevisiae. |
Family and domain databases | |
| Gene3D | 1.10.1040.10. 1 hit. 3.40.50.720. 1 hit. |
| InterPro | IPR008927. 6-PGluconate_DH_C-like. IPR013328. DH_multihelical. IPR006168. G3P_DH_NAD-dep. IPR006109. G3P_DH_NAD-dep_C. IPR017751. G3P_DH_NAD-dep_euk. IPR011128. G3P_DH_NAD-dep_N. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR11728. PTHR11728. 1 hit. |
| Pfam | PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. [Graphical view] |
| PRINTS | PR00077. GPDHDRGNASE. |
| SUPFAM | SSF48179. 6DGDH_C_like. 1 hit. |
| TIGRFAMs | TIGR03376. glycerol3P_DH. 1 hit. |
| PROSITE | PS00957. NAD_G3PDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 975758. |
Entry information
| Entry name | GPD2_YEAST | ||||||||
| Accession | Primary (citable) accession number: P41911 Secondary accession number(s): D6W208, P50905 | ||||||||
| 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 XV Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
