Glyceraldehyde-3-phosphate dehydrogenase 3 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P00359 (G3P3_YEAST)

Last modified June 16, 2009. Version 109. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 3
      Short name=GAPDH 3
    EC=1.2.1.12

Gene names

Name:	TDH3
Synonyms:	GPD3
Ordered Locus Names:	YGR192C
ORF Names:	G7576

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NAD⁺ = 3-phospho-D-glyceroyl phosphate + NADH.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm. Ref.7
Miscellaneous	There are three genes for G3PDH in yeast. Present with 169000 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptosis Inferred from mutant phenotype. Source: SGD gluconeogenesis Inferred from expression pattern. Source: SGD glycolysis Inferred from expression pattern. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen and reactive oxygen species metabolic process Inferred from mutant phenotype. Source: SGD
Cellular component	fungal-type cell wall Inferred from direct assay. Source: SGD lipid particle Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
	Q04170	1	EBI-7218,EBI-31721
	Q7M4S9	1	EBI-7218,EBI-375733
FMT1	P32785	1	EBI-7218,EBI-7033
SRP1	Q02821	1	EBI-7218,EBI-1797

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 332

331

Glyceraldehyde-3-phosphate dehydrogenase 3

PRO_0000145591

Regions

Nucleotide binding

11 – 12

NAD By similarity

Region

149 – 151

Glyceraldehyde 3-phosphate binding By similarity

Region

209 – 210

Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site

150

Nucleophile By similarity

Binding site

NAD By similarity

Binding site

NAD; via carbonyl oxygen By similarity

Binding site

180

Glyceraldehyde 3-phosphate By similarity

Binding site

232

Glyceraldehyde 3-phosphate By similarity

Binding site

314

NAD By similarity

Site

177

Activates thiol group during catalysis By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.12

Modified residue

123

Phosphoserine Ref.12

Modified residue

124

Phosphoserine Ref.12

Modified residue

125

Phosphothreonine Ref.12

Modified residue

149

Phosphoserine Ref.12 Ref.9

Modified residue

151

Phosphothreonine Ref.12

Modified residue

152

Phosphothreonine Ref.12

Modified residue

175

Phosphothreonine Ref.10

Modified residue

178

Phosphoserine Ref.12 Ref.9 Ref.10

Modified residue

182

Phosphothreonine Ref.12

Modified residue

190

Phosphoserine Ref.12

Modified residue

199

Phosphothreonine Ref.12

Modified residue

201

Phosphoserine Ref.12 Ref.9

Modified residue

207

Phosphoserine Ref.12

Modified residue

208

Phosphoserine Ref.12

Modified residue

209

Phosphothreonine Ref.12

Modified residue

227

Phosphothreonine Ref.12 Ref.11

Modified residue

235

Phosphothreonine Ref.12

Modified residue

239

Phosphoserine Ref.12

Modified residue

252

Phosphothreonine Ref.12

Modified residue

302

Phosphoserine Ref.12

Modified residue

310

Phosphoserine Ref.12

Modified residue

312

Phosphotyrosine Ref.12

Experimental info

Sequence conflict

136

E → V in CAA24607. Ref.1

Sequence conflict

136

E → V in AAA88714. Ref.1

Sequence conflict

248

N → D in CAA24607. Ref.1

Sequence conflict

248

N → D in AAA88714. Ref.1

Sequence conflict

287

D → G in AAS56157. Ref.4

Sequence conflict

329

V → I in CAA24607. Ref.1

Sequence conflict

329

V → I in AAA88714. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P00359-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6CFFFEE7061BC36F
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FASTA

332

35,747

        10         20         30         40         50         60 
MVRVAINGFG RIGRLVMRIA LSRPNVEVVA LNDPFITNDY AAYMFKYDST HGRYAGEVSH 

        70         80         90        100        110        120 
DDKHIIVDGK KIATYQERDP ANLPWGSSNV DIAIDSTGVF KELDTAQKHI DAGAKKVVIT 

       130        140        150        160        170        180 
APSSTAPMFV MGVNEEKYTS DLKIVSNASC TTNCLAPLAK VINDAFGIEE GLMTTVHSLT 

       190        200        210        220        230        240 
ATQKTVDGPS HKDWRGGRTA SGNIIPSSTG AAKAVGKVLP ELQGKLTGMA FRVPTVDVSV 

       250        260        270        280        290        300 
VDLTVKLNKE TTYDEIKKVV KAAAEGKLKG VLGYTEDAVV SSDFLGDSHS SIFDASAGIQ 

       310        320        330 
LSPKFVKLVS WYDNEYGYST RVVDLVEHVA KA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 385592] [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: 7645350] [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. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed: 7895733] [Abstract] Cited for: PROTEIN SEQUENCE OF 47-58. Strain: ATCC 204508 / S288c.
[6]	"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: 7737086] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Strain: ATCC 38531 / Y41 and ATCC 44827 / SKQ2N.
[7]	"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: 11502169] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"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].
[9]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-178 AND SER-201, MASS SPECTROMETRY.
[10]	"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 THR-175 AND SER-178, MASS SPECTROMETRY.
[11]	"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 THR-227, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-123; SER-124; THR-125; SER-149; THR-151; THR-152; SER-178; THR-182; SER-190; THR-199; SER-201; SER-207; SER-208; THR-209; THR-227; THR-235; SER-239; THR-252; SER-302; SER-310 AND TYR-312, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	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.
PIR	DEBYG2. S55870.
RefSeq	NP_011708.1.
3D structure databases
HSSP	HSSP built from PDB template 1DC5 based on UniProtKB P06977.
SMR	P00359. Positions 1-330.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4309N.
IntAct	P00359. 99 interactions.
2-D gel databases
SWISS-2DPAGE	P00359.
COMPLUYEAST-2DPAGE	P00359.
Proteomic databases
PeptideAtlas	P00359.
PRIDE	P00359.
Genome annotation databases
Ensembl	YGR192C. Saccharomyces cerevisiae. [Contig view]
GeneID	853106.
GenomeReviews	Gene locus YGR192C in contig Y13135_GR.
KEGG	sce:YGR192C.
NMPDR	fig\|4932.3.peg.2835.
Organism-specific databases
CYGD	YGR192c.
SGD	S000003424. TDH3.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P00359.
OMA	P00359. IGANENS.
Enzyme and pathway databases
BRENDA	1.2.1.12. 250.
Gene expression databases
GermOnline	YGR192C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000173. GlycerAld_3-P_DH. IPR006424. Glyceraldehyde-3-P_DH_1. [Graphical view]
PANTHER	PTHR10836. GAP_DH. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
PRINTS	PR00078. G3PDHDRGNASE.
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	973112.

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Entry information

Entry name

G3P3_YEAST

Accession

Primary (citable) accession number: P00359
Secondary accession number(s): Q6Q5P9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome VII

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents