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P41911

- GPD2_YEAST

UniProt

P41911 - GPD2_YEAST

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Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, mitochondrial

Gene

GPD2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei178 – 1781NADBy similarity
Binding sitei201 – 2011NAD; via amide nitrogenBy similarity
Binding sitei201 – 2011SubstrateBy similarity
Binding sitei234 – 2341NAD; via amide nitrogenBy similarity
Active sitei294 – 2941Proton acceptorBy similarity
Binding sitei359 – 3591NADBy similarity
Binding sitei388 – 3881NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi90 – 956NADBy similarity

GO - Molecular functioni

  1. glycerol-3-phosphate dehydrogenase [NAD+] activity Source: SGD
  2. NAD binding Source: InterPro

GO - Biological processi

  1. glycerol-3-phosphate catabolic process Source: InterPro
  2. glycerol metabolic process Source: SGD
  3. NADH oxidation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciYEAST:YOL059W-MONOMER.
ReactomeiREACT_191569. Synthesis of PA.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, mitochondrial (EC:1.1.1.8)
Gene namesi
Name:GPD2
Synonyms:GPD3
Ordered Locus Names:YOL059W
ORF Names:O1222
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOL059w.
SGDiS000005420. GPD2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
  2. glycerol-3-phosphate dehydrogenase complex Source: InterPro
  3. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1616MitochondrionSequence AnalysisAdd
BLAST
Chaini17 – 440424Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, mitochondrialPRO_0000043410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701Phosphoserine1 Publication
Modified residuei72 – 721Phosphoserine5 Publications
Modified residuei75 – 751Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41911.
PaxDbiP41911.
PeptideAtlasiP41911.

Expressioni

Inductioni

By anaerobic growth conditions and other conditions leading to accumulation of cytosolic NADH.2 Publications

Gene expression databases

GenevestigatoriP41911.

Interactioni

Protein-protein interaction databases

BioGridi34342. 56 interactions.
DIPiDIP-1348N.
IntActiP41911. 5 interactions.
MINTiMINT-411876.
STRINGi4932.YOL059W.

Structurei

3D structure databases

ProteinModelPortaliP41911.
SMRiP41911. Positions 83-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni359 – 3602Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0240.
GeneTreeiENSGT00390000003114.
HOGENOMiHOG000246855.
InParanoidiP41911.
KOiK00006.
OMAiQIVYNNV.
OrthoDBiEOG7V76H7.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 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]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P41911-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLAVRRLTRY TFLKRTHPVL YTRRAYKILP SRSTFLRRSL LQTQLHSKMT
60 70 80 90 100
AHTNIKQHKH CHEDHPIRRS DSAVSIVHLK RAPFKVTVIG SGNWGTTIAK
110 120 130 140 150
VIAENTELHS HIFEPEVRMW VFDEKIGDEN LTDIINTRHQ NVKYLPNIDL
160 170 180 190 200
PHNLVADPDL LHSIKGADIL VFNIPHQFLP NIVKQLQGHV APHVRAISCL
210 220 230 240 250
KGFELGSKGV QLLSSYVTDE LGIQCGALSG ANLAPEVAKE HWSETTVAYQ
260 270 280 290 300
LPKDYQGDGK DVDHKILKLL FHRPYFHVNV IDDVAGISIA GALKNVVALA
310 320 330 340 350
CGFVEGMGWG NNASAAIQRL GLGEIIKFGR MFFPESKVET YYQESAGVAD
360 370 380 390 400
LITTCSGGRN VKVATYMAKT GKSALEAEKE LLNGQSAQGI ITCREVHEWL
410 420 430 440
QTCELTQEFP LFEAVYQIVY NNVRMEDLPE MIEELDIDDE
Length:440
Mass (Da):49,422
Last modified:October 1, 1996 - v2
Checksum:iFA6C07034D3EC720
GO

Sequence cautioni

The sequence CAA84532.1 differs from that shown. Reason: Frameshift at position 411.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS61719.
RefSeqiNP_014582.1. NM_001183314.1.

Genome annotation databases

EnsemblFungiiYOL059W; YOL059W; YOL059W.
GeneIDi854095.
KEGGisce:YOL059W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S61719.
RefSeqi NP_014582.1. NM_001183314.1.

3D structure databases

ProteinModelPortali P41911.
SMRi P41911. Positions 83-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34342. 56 interactions.
DIPi DIP-1348N.
IntActi P41911. 5 interactions.
MINTi MINT-411876.
STRINGi 4932.YOL059W.

Proteomic databases

MaxQBi P41911.
PaxDbi P41911.
PeptideAtlasi P41911.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOL059W ; YOL059W ; YOL059W .
GeneIDi 854095.
KEGGi sce:YOL059W.

Organism-specific databases

CYGDi YOL059w.
SGDi S000005420. GPD2.

Phylogenomic databases

eggNOGi COG0240.
GeneTreei ENSGT00390000003114.
HOGENOMi HOG000246855.
InParanoidi P41911.
KOi K00006.
OMAi QIVYNNV.
OrthoDBi EOG7V76H7.

Enzyme and pathway databases

BioCyci YEAST:YOL059W-MONOMER.
Reactomei REACT_191569. Synthesis of PA.

Miscellaneous databases

NextBioi 975758.

Gene expression databases

Genevestigatori P41911.

Family and domain databases

Gene3Di 1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProi 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 ]
PANTHERi PTHR11728. PTHR11728. 1 hit.
Pfami PF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view ]
PRINTSi PR00077. GPDHDRGNASE.
SUPFAMi SSF48179. SSF48179. 1 hit.
TIGRFAMsi TIGR03376. glycerol3P_DH. 1 hit.
PROSITEi PS00957. NAD_G3PDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION.
  12. "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-72 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-72 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGPD2_YEAST
AccessioniPrimary (citable) accession number: P41911
Secondary accession number(s): D6W208, P50905
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8966 molecules/cell in log phase SD medium.1 Publication

Caution

It is uncertain whether Met-1 or Met-49 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3