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P00359

- G3P3_YEAST

UniProt

P00359 - G3P3_YEAST

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Protein
Glyceraldehyde-3-phosphate dehydrogenase 3
Gene
TDH3, GPD3, YGR192C, G7576
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331NAD By similarity
Binding sitei78 – 781NAD; via carbonyl oxygen By similarity
Active sitei150 – 1501Nucleophile By similarity
Sitei177 – 1771Activates thiol group during catalysis By similarity
Binding sitei180 – 1801Glyceraldehyde 3-phosphate By similarity
Binding sitei232 – 2321Glyceraldehyde 3-phosphate By similarity
Binding sitei314 – 3141NAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 122NAD By similarity

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. NADP binding Source: InterPro
  3. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: SGD

GO - Biological processi

  1. apoptotic process Source: SGD
  2. gluconeogenesis Source: SGD
  3. glycolytic process Source: SGD
  4. reactive oxygen species metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciYEAST:YGR192C-MONOMER.
SABIO-RKP00359.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase 3 (EC:1.2.1.12)
Short name:
GAPDH 3
Gene namesi
Name:TDH3
Synonyms:GPD3
Ordered Locus Names:YGR192C
ORF Names:G7576
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

SGDiS000003424. TDH3.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. fungal-type cell wall Source: SGD
  3. lipid particle Source: SGD
  4. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 332331Glyceraldehyde-3-phosphate dehydrogenase 3
PRO_0000145591Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei302 – 3021Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00359.
PaxDbiP00359.
PeptideAtlasiP00359.
PRIDEiP00359.

2D gel databases

COMPLUYEAST-2DPAGEP00359.
SWISS-2DPAGEP00359.

Expressioni

Gene expression databases

GenevestigatoriP00359.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi33445. 153 interactions.
DIPiDIP-4309N.
IntActiP00359. 100 interactions.
MINTiMINT-8285236.
STRINGi4932.YGR192C.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75
Helixi11 – 2212
Beta strandi27 – 326
Helixi38 – 469
Turni49 – 513
Beta strandi58 – 603
Beta strandi62 – 676
Beta strandi70 – 756
Helixi80 – 823
Turni85 – 895
Beta strandi91 – 955
Beta strandi97 – 1004
Helixi103 – 1119
Beta strandi115 – 1217
Beta strandi124 – 1263
Turni131 – 1333
Helixi135 – 1373
Beta strandi144 – 1463
Helixi150 – 16617
Beta strandi168 – 17811
Beta strandi183 – 1875
Helixi195 – 1973
Helixi200 – 2023
Beta strandi205 – 2084
Helixi211 – 2188
Helixi220 – 2223
Beta strandi225 – 23410
Beta strandi239 – 24911
Helixi253 – 26513
Turni266 – 2716
Beta strandi272 – 2754
Helixi281 – 2844
Beta strandi290 – 2945
Helixi295 – 2973
Beta strandi299 – 3024
Beta strandi305 – 3128
Helixi316 – 33116

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PYMX-ray2.00A/B1-332[»]
4IQ8X-ray2.49A1-332[»]
ProteinModelPortaliP00359.
SMRiP00359. Positions 1-332.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1513Glyceraldehyde 3-phosphate binding By similarity
Regioni209 – 2102Glyceraldehyde 3-phosphate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0057.
GeneTreeiENSGT00720000108591.
HOGENOMiHOG000071678.
KOiK00134.
OMAiINDIMDI.
OrthoDBiEOG70W3Q6.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00359-1 [UniParc]FASTAAdd to Basket

« Hide

MVRVAINGFG RIGRLVMRIA LSRPNVEVVA LNDPFITNDY AAYMFKYDST    50
HGRYAGEVSH DDKHIIVDGK KIATYQERDP ANLPWGSSNV DIAIDSTGVF 100
KELDTAQKHI DAGAKKVVIT APSSTAPMFV MGVNEEKYTS DLKIVSNASC 150
TTNCLAPLAK VINDAFGIEE GLMTTVHSLT ATQKTVDGPS HKDWRGGRTA 200
SGNIIPSSTG AAKAVGKVLP ELQGKLTGMA FRVPTVDVSV VDLTVKLNKE 250
TTYDEIKKVV KAAAEGKLKG VLGYTEDAVV SSDFLGDSHS SIFDASAGIQ 300
LSPKFVKLVS WYDNEYGYST RVVDLVEHVA KA 332
Length:332
Mass (Da):35,747
Last modified:January 23, 2007 - v3
Checksum:i6CFFFEE7061BC36F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361E → V in CAA24607. 1 Publication
Sequence conflicti136 – 1361E → V in AAA88714. 1 Publication
Sequence conflicti248 – 2481N → D in CAA24607. 1 Publication
Sequence conflicti248 – 2481N → D in AAA88714. 1 Publication
Sequence conflicti287 – 2871D → G in AAS56157. 1 Publication
Sequence conflicti329 – 3291V → I in CAA24607. 1 Publication
Sequence conflicti329 – 3291V → I in AAA88714. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V01300 Genomic DNA. Translation: CAA24607.1.
J01324 Genomic DNA. Translation: AAA88714.1.
X82408 Genomic DNA. Translation: CAA57803.1.
Z72977 Genomic DNA. Translation: CAA97218.1.
AY557831 Genomic DNA. Translation: AAS56157.1.
BK006941 Genomic DNA. Translation: DAA08285.1.
PIRiS55870. DEBYG2.
RefSeqiNP_011708.3. NM_001181321.3.

Genome annotation databases

EnsemblFungiiYGR192C; YGR192C; YGR192C.
GeneIDi853106.
KEGGisce:YGR192C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V01300 Genomic DNA. Translation: CAA24607.1 .
J01324 Genomic DNA. Translation: AAA88714.1 .
X82408 Genomic DNA. Translation: CAA57803.1 .
Z72977 Genomic DNA. Translation: CAA97218.1 .
AY557831 Genomic DNA. Translation: AAS56157.1 .
BK006941 Genomic DNA. Translation: DAA08285.1 .
PIRi S55870. DEBYG2.
RefSeqi NP_011708.3. NM_001181321.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3PYM X-ray 2.00 A/B 1-332 [» ]
4IQ8 X-ray 2.49 A 1-332 [» ]
ProteinModelPortali P00359.
SMRi P00359. Positions 1-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33445. 153 interactions.
DIPi DIP-4309N.
IntActi P00359. 100 interactions.
MINTi MINT-8285236.
STRINGi 4932.YGR192C.

2D gel databases

COMPLUYEAST-2DPAGE P00359.
SWISS-2DPAGE P00359.

Proteomic databases

MaxQBi P00359.
PaxDbi P00359.
PeptideAtlasi P00359.
PRIDEi P00359.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR192C ; YGR192C ; YGR192C .
GeneIDi 853106.
KEGGi sce:YGR192C.

Organism-specific databases

SGDi S000003424. TDH3.

Phylogenomic databases

eggNOGi COG0057.
GeneTreei ENSGT00720000108591.
HOGENOMi HOG000071678.
KOi K00134.
OMAi INDIMDI.
OrthoDBi EOG70W3Q6.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00184 .
BioCyci YEAST:YGR192C-MONOMER.
SABIO-RK P00359.

Miscellaneous databases

NextBioi 973112.
PROi P00359.

Gene expression databases

Genevestigatori P00359.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR10836. PTHR10836. 1 hit.
Pfami PF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000149. GAP_DH. 1 hit.
PRINTSi PR00078. G3PDHDRGNASE.
SMARTi SM00846. Gp_dh_N. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01534. GAPDH-I. 1 hit.
PROSITEi PS00071. GAPDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of a glyceraldehyde-3-phosphate dehydrogenase gene from Saccharomyces cerevisiae."
    Holland J.P., Holland M.J.
    J. Biol. Chem. 254:9839-9845(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete sequence of a 9037 bp DNA fragment of the right arm of Saccharomyces cerevisiae chromosome VII."
    Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C.
    Yeast 11:587-591(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(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. "Glyceraldehyde 3-phosphate dehydrogenase: Amino acid sequence of enzyme from baker's yeast."
    Jones G.M., Harris J.I.
    FEBS Lett. 22:185-189(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE OF 2-332, CLEAVAGE OF INITIATOR METHIONINE.
  7. Cited for: PROTEIN SEQUENCE OF 47-58.
    Strain: ATCC 204508 / S288c.
  8. "Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides."
    Norbeck J., Blomberg A.
    Electrophoresis 16:149-156(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 38531 / Y41 and ATCC 44827 / SKQ2N.
  9. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
    Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
    Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Structure of GAPDH 3 from S.cerevisiae at 2.0 A resolution."
    Garcia-Saez I., Kozielski F., Job D., Boscheron C.
    Submitted (DEC-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
  16. "Preliminary crystallographic analysis of glyceraldehyde-3-phosphate dehydrogenase 3 from Saccharomyces cerevisiae."
    Liu Q., Wang H., Liu H., Teng M., Li X.
    Acta Crystallogr. F 68:978-980(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiG3P3_YEAST
AccessioniPrimary (citable) accession number: P00359
Secondary accession number(s): D6VUX4, Q6Q5P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are three genes for G3PDH in yeast.
Present with 169000 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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