Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P41911 (GPD2_YEAST)

Last modified February 9, 2010. Version 100. 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial
    EC=1.1.1.8
Gene names
Name: GPD2
Synonyms: GPD3
Ordered Locus Names: YOL059W
ORF Names: O1222
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length440 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 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

Cytoplasm. Mitochondrion Ref.8 Ref.10 Ref.11.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1616Mitochondrion Potential
Chain17 – 440424Glycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial
PRO_0000043410

Regions

Nucleotide binding90 – 956NAD By similarity
Region359 – 3602Substrate binding By similarity

Sites

Active site2941Proton acceptor By similarity
Binding site1781NAD By similarity
Binding site2011NAD; via amide nitrogen By similarity
Binding site2011Substrate By similarity
Binding site2341NAD; via amide nitrogen By similarity
Binding site3591NAD By similarity
Binding site3881NAD By similarity

Amino acid modifications

Modified residue701Phosphoserine Ref.13 Ref.15
Modified residue721Phosphoserine Ref.13 Ref.15 Ref.7 Ref.12 Ref.14
Modified residue751Phosphoserine Ref.13 Ref.15 Ref.7 Ref.12 Ref.14

Sequences

Sequence LengthMass (Da)Tools
P41911-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: FA6C07034D3EC720

FASTA44049,422
        10         20         30         40         50         60 
MLAVRRLTRY TFLKRTHPVL YTRRAYKILP SRSTFLRRSL LQTQLHSKMT AHTNIKQHKH 

        70         80         90        100        110        120 
CHEDHPIRRS DSAVSIVHLK RAPFKVTVIG SGNWGTTIAK VIAENTELHS HIFEPEVRMW 

       130        140        150        160        170        180 
VFDEKIGDEN LTDIINTRHQ NVKYLPNIDL PHNLVADPDL LHSIKGADIL VFNIPHQFLP 

       190        200        210        220        230        240 
NIVKQLQGHV APHVRAISCL KGFELGSKGV QLLSSYVTDE LGIQCGALSG ANLAPEVAKE 

       250        260        270        280        290        300 
HWSETTVAYQ LPKDYQGDGK DVDHKILKLL FHRPYFHVNV IDDVAGISIA GALKNVVALA 

       310        320        330        340        350        360 
CGFVEGMGWG NNASAAIQRL GLGEIIKFGR MFFPESKVET YYQESAGVAD LITTCSGGRN 

       370        380        390        400        410        420 
VKVATYMAKT GKSALEAEKE LLNGQSAQGI ITCREVHEWL QTCELTQEFP LFEAVYQIVY 

       430        440 
NNVRMEDLPE MIEELDIDDE 

« Hide

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. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., 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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., 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

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.
PIRS61719.
RefSeqNP_014582.1.

3D structure databases

SMRP41911. Positions 82-431.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1348N.
IntActP41911. 12 interactions.
STRINGP41911.

Proteomic databases

PeptideAtlasP41911.

Genome annotation databases

EnsemblYOL059W; YOL059W; YOL059W; Saccharomyces cerevisiae. [Genome view]
GeneID854095.
KEGGsce:YOL059W.
NMPDRfig|4932.3.peg.5674.

Organism-specific databases

CYGDYOL059w.
SGDS000005420. GPD2.

Phylogenomic databases

eggNOGfuNOG04977.
HOGENOMHBG586392.
OMATHESAGV.
OrthoDBEOG9J9PGK.
PhylomeDBP41911.

Enzyme and pathway databases

BRENDA1.1.1.8. 250.

Gene expression databases

ArrayExpressP41911.
GenevestigatorP41911.
GermOnlineYOL059W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR008927. 6-PGluconate_DH_C-like.
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]
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]
PRINTSPR00077. GPDHDRGNASE.
TIGRFAMsTIGR03376. glycerol3P_DH. 1 hit.
PROSITEPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio975758.

Entry information

Entry nameGPD2_YEAST
AccessionPrimary (citable) accession number: P41911
Secondary accession number(s): P50905
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: February 9, 2010
This is version 100 of the entry and version 2 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents