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Reviewed, UniProtKB/Swiss-Prot Q00055 (GPD1_YEAST)

Last modified November 25, 2008. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycerol-3-phosphate dehydrogenase [NAD+] 1
    EC=1.1.1.8
Gene names
Name: GPD1
Synonyms: DAR1, HOR1, OSG1
Ordered Locus Names: YDL022W
ORF Names: D2830
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the production and accumulation of glycerol during hyperosmotic stress conditions. Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells.

Catalytic activity

sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH.

Subcellular location

Cytoplasm. Peroxisome.

Induction

By osmotic stress and by methylglyoxal in a HOG pathway-dependent manner.

Miscellaneous

Present with 807 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.

Caution

Was originally (Ref.6) thought to be GUT2, the FAD-dependent glycerol-3-phosphate dehydrogenase.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 391390Glycerol-3-phosphate dehydrogenase [NAD+] 1
PRO_0000138100

Regions

Nucleotide binding41 – 466NAD By similarity
Region310 – 3112Substrate binding By similarity

Sites

Active site2451Proton acceptor By similarity
Binding site1291NAD By similarity
Binding site1521NAD; via amide nitrogen By similarity
Binding site1521Substrate By similarity
Binding site1851NAD; via amide nitrogen By similarity
Binding site3101NAD By similarity
Binding site3391NAD By similarity

Amino acid modifications

Modified residue21N-acetylserine
Modified residue121Phosphoserine
Modified residue231Phosphoserine
Modified residue241Phosphoserine
Modified residue251Phosphoserine
Modified residue271Phosphoserine

Natural variations

Natural variant161N → D in strain: WFB.
Natural variant1431S → A in strain: WFB.
Natural variant1641L → P in strain: WFB.
Natural variant1831N → S in strain: WFB.
Natural variant2251P → S in strain: WFB.
Natural variant2561E → V in strain: WFB.

Experimental info

Sequence conflict103 – 1075DNLVA → TIWLL in AAA18631. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q00055-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: F5F1F7F111F707D1

FASTA39142,869
        10         20         30         40         50         60 
MSAAADRLNL TSGHLNAGRK RSSSSVSLKA AEKPFKVTVI GSGNWGTTIA KVVAENCKGY 

        70         80         90        100        110        120 
PEVFAPIVQM WVFEEEINGE KLTEIINTRH QNVKYLPGIT LPDNLVANPD LIDSVKDVDI 

       130        140        150        160        170        180 
IVFNIPHQFL PRICSQLKGH VDSHVRAISC LKGFEVGAKG VQLLSSYITE ELGIQCGALS 

       190        200        210        220        230        240 
GANIATEVAQ EHWSETTVAY HIPKDFRGEG KDVDHKVLKA LFHRPYFHVS VIEDVAGISI 

       250        260        270        280        290        300 
CGALKNVVAL GCGFVEGLGW GNNASAAIQR VGLGEIIRFG QMFFPESREE TYYQESAGVA 

       310        320        330        340        350        360 
DLITTCAGGR NVKVARLMAT SGKDAWECEK ELLNGQSAQG LITCKEVHEW LETCGSVEDF 

       370        380        390 
PLFEAVYQIV YNNYPMKNLP DMIEELDLHE D 

« Hide

References

« Hide 'large scale' references
[1]"A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements an osmosensitive mutant of Saccharomyces cerevisiae."
Larsson K., Ansell R., Eriksson P., Adler L.
Mol. Microbiol. 10:1101-1111(1993) [PubMed: 7934860] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-49.
[2]"GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway."
Albertyn J., Hohmann S., Thevelein J.M., Prior B.A.
Mol. Cell. Biol. 14:4135-4144(1994) [PubMed: 8196651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
[3]"Cloning, sequence, and disruption of the Saccharomyces diastaticus DAR1 gene encoding a glycerol-3-phosphate dehydrogenase."
Wang H.T., Rahaim P., Robbins P., Yocum R.R.
J. Bacteriol. 176:7091-7095(1994) [PubMed: 7961476] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Diastaticus / ATCC 62933 / NRC 5704 / J132b.
[4]"Research on the mechanism of osmotolerance and thermotolerance of yeast."
Ma X., Guo Y., Zhang F., Yu H., Kuang J., Yao J., Li Z., He G.
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-16; ALA-143; PRO-164; SER-183; SER-225 AND VAL-256.
Strain: FHS and WFB.
[5]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Cloning and characterisation of the Saccharomyces cerevisiae glycerol-3-phosphate dehydrogenase (GUT2) promoter."
Sleep D., Ogden J.E., Roberts N.A., Goodey A.R.
Gene 101:89-96(1991) [PubMed: 1676389] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
[7]Bienvenut W.V., Peters C.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-19 AND 271-278, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY.
[8]"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
Norbeck J., Blomberg A.
FEMS Microbiol. Lett. 137:1-8(1996) [PubMed: 8935650] [Abstract]
Cited for: PROTEIN SEQUENCE OF 8-16; 95-108 AND 160-173.
Strain: ATCC 38531 / Y41.
[9]"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-24 AND SER-27, MASS SPECTROMETRY.
[10]"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].
[11]"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].
[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: 15210723] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"The HOG MAP kinase pathway is required for the induction of methylglyoxal-responsive genes and determines methylglyoxal resistance in Saccharomyces cerevisiae."
Aguilera J., Rodriguez-Vargas S., Prieto J.A.
Mol. Microbiol. 56:228-239(2005) [PubMed: 15773992] [Abstract]
Cited for: INDUCTION.
[14]"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-24 AND SER-27, 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: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-27, 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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-24; SER-25 AND SER-27, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

Z24454 Genomic DNA. Translation: CAA80827.1.
X76859 Genomic DNA. Translation: CAA54189.1.
U04621 Genomic DNA. Translation: AAA64936.1.
AY598965 Genomic DNA. Translation: AAT27375.1.
AY598968 Genomic DNA. Translation: AAT27378.1.
Z48432 Genomic DNA. Translation: CAA88337.1.
Z74071 Genomic DNA. Translation: CAA98582.1.
M38740 Genomic DNA. Translation: AAA18631.1.
PIRS40059.
RefSeqNP_010262.1.

3D structure databases

HSSPHSSP built from PDB template 1EVY based on UniProtKB P90551.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6393N.

Proteomic databases

PeptideAtlasQ00055.

Genome annotation databases

EnsemblYDL022W. Saccharomyces cerevisiae. [Contig view]
GeneID851539.
KEGGsce:YDL022W.
NMPDRfig|4932.3.peg.1004.

Organism-specific databases

CYGDYDL022w.
SGDS000002180. GPD1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMQ00055.

Gene expression databases

ArrayExpressQ00055.
GermOnlineYDL022W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR013328. DHase_multihelical.
IPR016040. NAD(P)-bd.
IPR017751. NAD-dep_Gly3P_DH_euk.
IPR006168. NAD-dep_Gly3P_DHase.
IPR011128. NAD-dep_Gly3P_DHase_N.
IPR006109. NAD_Gly3P_DHase_C.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHERPTHR11728. NAD_Gly3P_DH. 1 hit.
PfamPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSPR00077. GPDHDRGNASE.
ProDomPD001278. NAD_Gly3P_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubQ00055.
NextBio968943.

Entry information

Entry nameGPD1_YEAST
AccessionPrimary (citable) accession number: Q00055
Secondary accession number(s): Q6J5J2, Q6J5J5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 92 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents