Reviewed, UniProtKB/Swiss-Prot Q00055 (GPD1_YEAST)

Names and origin

Protein names

Recommended 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

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	391 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 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.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm Peroxisome
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	NADH oxidation Inferred from mutant phenotype. Source: SGD carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro intracellular accumulation of glycerol Ref.2 Inferred from mutant phenotype. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.12 Inferred from direct assay. Source: SGD glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro peroxisome Ref.12 Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase (NAD+) activity Ref.2 Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 391	390	Glycerol-3-phosphate dehydrogenase [NAD+] 1		PRO_0000138100
Regions
	Nucleotide binding	41 – 46	6	NAD By similarity
	Region	310 – 311	2	Substrate binding By similarity
Sites
	Active site	245	1	Proton acceptor By similarity
	Binding site	129	1	NAD By similarity
	Binding site	152	1	NAD; via amide nitrogen By similarity
	Binding site	152	1	Substrate By similarity
	Binding site	185	1	NAD; via amide nitrogen By similarity
	Binding site	310	1	NAD By similarity
	Binding site	339	1	NAD By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine
	Modified residue	12	1	Phosphoserine
	Modified residue	23	1	Phosphoserine
	Modified residue	24	1	Phosphoserine
	Modified residue	25	1	Phosphoserine
	Modified residue	27	1	Phosphoserine
Natural variations
	Natural variant	16	1	N → D in strain: WFB.
	Natural variant	143	1	S → A in strain: WFB.
	Natural variant	164	1	L → P in strain: WFB.
	Natural variant	183	1	N → S in strain: WFB.
	Natural variant	225	1	P → S in strain: WFB.
	Natural variant	256	1	E → V in strain: WFB.
Experimental info
	Sequence conflict	103 – 107	5	DNLVA → TIWLL in AAA18631. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q00055-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: F5F1F7F111F707D1	FASTA	391	42,869
	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

References

	« Hide 'large scale' referencesShow '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. , 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
EMBLGenBankDDBJ	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.
PIR	S40059.
RefSeq	NP_010262.1.
3D structure databases
HSSP	HSSP built from PDB template 1EVY based on UniProtKB P90551.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6393N.
Proteomic databases
PeptideAtlas	Q00055.
Genome annotation databases
Ensembl	YDL022W. Saccharomyces cerevisiae. [Contig view]
GeneID	851539.
KEGG	sce:YDL022W.
NMPDR	fig|4932.3.peg.1004.
Organism-specific databases
CYGD	YDL022w.
SGD	S000002180. GPD1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q00055.
Gene expression databases
ArrayExpress	Q00055.
GermOnline	YDL022W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013328. 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]
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]
PIRSF	PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTS	PR00077. GPDHDRGNASE.
ProDom	PD001278. NAD_Gly3P_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	Q00055.
NextBio	968943.

Entry information

Entry name

GPD1_YEAST

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)