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Q00055 (GPD1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [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. Ref.2

Catalytic activity

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

Subcellular location

Cytoplasm. Peroxisome Ref.11 Ref.13.

Induction

By osmotic stress and by methylglyoxal in a HOG pathway-dependent manner. Ref.2 Ref.15

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.8) thought to be GUT2, the FAD-dependent glycerol-3-phosphate dehydrogenase.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
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 Ref.9
Modified residue241Phosphoserine Ref.16
Modified residue271Phosphoserine Ref.14 Ref.16 Ref.18

Natural variations

Natural variant161N → D in strain: WFB. Ref.4
Natural variant1431S → A in strain: WFB. Ref.4
Natural variant1641L → P in strain: WFB. Ref.4
Natural variant1831N → S in strain: WFB. Ref.4
Natural variant2251P → S in strain: WFB. Ref.4
Natural variant2561E → V in strain: WFB. Ref.4

Experimental info

Sequence conflict103 – 1075DNLVA → TIWLL in AAA18631. Ref.8

Secondary structure

................................................................ 391
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00055 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"The effects of co-expression of ScGPD1 and AtNHX1 on the salt tolerance of yeast."
Fu C., Zheng D.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
[9]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, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 8-16; 95-108 AND 160-173.
Strain: ATCC 38531 / Y41.
[11]"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].
[12]"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].
[13]"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.
[14]"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-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[15]"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] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[16]"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-24 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[17]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
EF596737 Genomic DNA. Translation: ABQ58864.1.
M38740 Genomic DNA. Translation: AAA18631.1.
BK006938 Genomic DNA. Translation: DAA11828.1.
PIRS40059.
RefSeqNP_010262.1. NM_001180081.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4FGWX-ray2.45A/B1-391[»]
ProteinModelPortalQ00055.
SMRQ00055. Positions 33-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32033. 55 interactions.
DIPDIP-6393N.
IntActQ00055. 3 interactions.
MINTMINT-2788005.
STRING4932.YDL022W.

Proteomic databases

PaxDbQ00055.
PeptideAtlasQ00055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL022W; YDL022W; YDL022W.
GeneID851539.
KEGGsce:YDL022W.

Organism-specific databases

SGDS000002180. GPD1.

Phylogenomic databases

eggNOGCOG0240.
GeneTreeENSGT00390000003114.
HOGENOMHOG000246855.
KOK00006.
OMAVAGISIC.
OrthoDBEOG7V76H7.

Enzyme and pathway databases

BioCycMetaCyc:YDL022W-MONOMER.
YEAST:YDL022W-MONOMER.
BRENDA1.1.1.8. 984.

Gene expression databases

GenevestigatorQ00055.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 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]
PANTHERPTHR11728. PTHR11728. 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.
SUPFAMSSF48179. SSF48179. 1 hit.
TIGRFAMsTIGR03376. glycerol3P_DH. 1 hit.
PROSITEPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968943.

Entry information

Entry nameGPD1_YEAST
AccessionPrimary (citable) accession number: Q00055
Secondary accession number(s): A5YWB0 expand/collapse secondary AC list , D6VRW8, Q6J5J2, Q6J5J5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references