Glyceraldehyde-3-phosphate dehydrogenase 1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P00360 (G3P1_YEAST)

Last modified June 16, 2009. Version 108. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · 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 1
      Short name=GAPDH 1
    EC=1.2.1.12

Gene names

Name:	TDH1
Synonyms:	GPD1, SSS2
Ordered Locus Names:	YJL052W
ORF Names:	J1154

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 not processed.
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.6
Miscellaneous	There are three genes for G3PDH in yeast. Present with 120000 molecules/cell in log phase SD medium. Ref.7
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	gluconeogenesis Inferred from expression pattern. Source: SGD glycolysis Inferred from expression pattern. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 332

332

Glyceraldehyde-3-phosphate dehydrogenase 1

PRO_0000145589

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

Phosphotyrosine Ref.10

Modified residue

124

Phosphoserine Ref.10

Modified residue

125

Phosphoserine Ref.10

Modified residue

149

Phosphoserine Ref.8

Modified residue

182

Phosphothreonine Ref.10

Modified residue

199

Phosphothreonine Ref.9

Modified residue

201

Phosphoserine Ref.8 Ref.9

Modified residue

207

Phosphoserine Ref.9

Modified residue

208

Phosphoserine Ref.9

Modified residue

291

Phosphoserine Ref.9

Modified residue

310

Phosphoserine Ref.9

Experimental info

Sequence conflict

248

E → A in CAA24609. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P00360-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4C116C86EAF3DB70
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FASTA

332

35,750

        10         20         30         40         50         60 
MIRIAINGFG RIGRLVLRLA LQRKDIEVVA VNDPFISNDY AAYMVKYDST HGRYKGTVSH 

        70         80         90        100        110        120 
DDKHIIIDGV KIATYQERDP ANLPWGSLKI DVAVDSTGVF KELDTAQKHI DAGAKKVVIT 

       130        140        150        160        170        180 
APSSSAPMFV VGVNHTKYTP DKKIVSNASC TTNCLAPLAK VINDAFGIEE GLMTTVHSMT 

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

       250        260        270        280        290        300 
VDLTVKLEKE ATYDQIKKAV KAAAEGPMKG VLGYTEDAVV SSDFLGDTHA SIFDASAGIQ 

       310        320        330 
LSPKFVKLIS WYDNEYGYSA RVVDLIEYVA KA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homologous nucleotide sequences at the 5' termini of messenger RNAs synthesized from the yeast enolase and glyceraldehyde-3-phosphate dehydrogenase gene families. The primary structure of a third yeast glyceraldehyde-3-phosphate dehydrogenase gene." Holland J.P., Labieniec L., Swimmer C., Holland M.J. J. Biol. Chem. 258:5291-5299(1983) [PubMed: 6833300] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"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.
[4]	"Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins." Norbeck J., Blomberg A. Yeast 13:1519-1534(1997) [PubMed: 9509572] [Abstract] Cited for: PROTEIN SEQUENCE OF 64-70 AND 218-225. Strain: ATCC 44827 / SKQ2N.
[5]	"Divergence of glyceraldehyde-3-phosphate dehydrogenase isozymes in Saccharomyces cerevisiae complex." Kadokura T., Ito T., Takano S., Nakazato A., Hara H., Watanabe S., Kudo T., Takeda M., Kaneko T. Syst. Appl. Microbiol. 23:198-205(2000) [PubMed: 10930071] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
[6]	"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.
[7]	"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].
[8]	"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 AND SER-201, MASS SPECTROMETRY.
[9]	"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-199; SER-201; SER-207; SER-208; SER-291 AND SER-310, MASS SPECTROMETRY.
[10]	"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 TYR-43; SER-124; SER-125 AND THR-182, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	V01302 Genomic DNA. Translation: CAA24609.1. Z49327 Genomic DNA. Translation: CAA89343.1. AY693001 Genomic DNA. Translation: AAT93020.1.
PIR	DEBYG3. S56824.
RefSeq	NP_012483.1.
3D structure databases
HSSP	HSSP built from PDB template 1DC5 based on UniProtKB P06977.
SMR	P00360. Positions 1-330.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4304N.
IntAct	P00360. 19 interactions.
2-D gel databases
SWISS-2DPAGE	P00360.
COMPLUYEAST-2DPAGE	P00360.
Proteomic databases
PeptideAtlas	P00360.
PRIDE	P00360.
Genome annotation databases
Ensembl	YJL052W. Saccharomyces cerevisiae. [Contig view]
GeneID	853395.
GenomeReviews	Gene locus YJL052W in contig Y13136_GR.
KEGG	sce:YJL052W.
NMPDR	fig\|4932.3.peg.3456.
Organism-specific databases
CYGD	YJL052w.
SGD	S000003588. TDH1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P00360.
OMA	P00360. MIRIAIN.
Enzyme and pathway databases
BRENDA	1.2.1.12. 250.
Gene expression databases
GermOnline	YJL052W. 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	973876.

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Entry information

Entry name

G3P1_YEAST

Accession

Primary (citable) accession number: P00360

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 108 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 X

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

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