P00359 (G3P3_YEAST) Reviewed, UniProtKB/Swiss-Prot

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

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

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.8.
Miscellaneous	There are three genes for G3PDH in yeast. Present with 169000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from mutant phenotype PubMed 17726063. Source: SGD gluconeogenesis Inferred from expression pattern PubMed 3905788. Source: SGD glycolysis Inferred from expression pattern PubMed 3905788. Source: SGD reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 17726063. Source: SGD
Cellular_component	fungal-type cell wall Inferred from direct assay PubMed 11158358. Source: SGD lipid particle Inferred from direct assay PubMed 10515935. Source: SGD mitochondrion Inferred from direct assay PubMed 16823961PubMed 16962558. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Inferred from direct assay PubMed 3905788. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 332

331

Glyceraldehyde-3-phosphate dehydrogenase 3

PRO_0000145591

Regions

Nucleotide binding

11 – 12

2

NAD By similarity

Region

149 – 151

3

Glyceraldehyde 3-phosphate binding By similarity

Region

209 – 210

2

Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site

150

1

Nucleophile By similarity

Binding site

33

1

NAD By similarity

Binding site

78

1

NAD; via carbonyl oxygen By similarity

Binding site

180

1

Glyceraldehyde 3-phosphate By similarity

Binding site

232

1

Glyceraldehyde 3-phosphate By similarity

Binding site

314

1

NAD By similarity

Site

177

1

Activates thiol group during catalysis By similarity

Amino acid modifications

Modified residue

22

1

Phosphoserine Ref.13

Modified residue

123

1

Phosphoserine Ref.13

Modified residue

124

1

Phosphoserine Ref.13

Modified residue

125

1

Phosphothreonine Ref.13

Modified residue

149

1

Phosphoserine Ref.10 Ref.13

Modified residue

151

1

Phosphothreonine Ref.13

Modified residue

152

1

Phosphothreonine Ref.13

Modified residue

175

1

Phosphothreonine Ref.11

Modified residue

178

1

Phosphoserine Ref.10 Ref.11 Ref.13

Modified residue

182

1

Phosphothreonine Ref.13

Modified residue

190

1

Phosphoserine Ref.13

Modified residue

199

1

Phosphothreonine Ref.13

Modified residue

201

1

Phosphoserine Ref.10 Ref.13

Modified residue

207

1

Phosphoserine Ref.13

Modified residue

208

1

Phosphoserine Ref.13

Modified residue

209

1

Phosphothreonine Ref.13

Modified residue

227

1

Phosphothreonine Ref.12 Ref.13

Modified residue

235

1

Phosphothreonine Ref.13

Modified residue

239

1

Phosphoserine Ref.13

Modified residue

252

1

Phosphothreonine Ref.13

Modified residue

302

1

Phosphoserine Ref.13

Modified residue

310

1

Phosphoserine Ref.13

Modified residue

312

1

Phosphotyrosine Ref.13

Experimental info

Sequence conflict

136

1

E → V in CAA24607. Ref.1

Sequence conflict

136

1

E → V in AAA88714. Ref.1

Sequence conflict

248

1

N → D in CAA24607. Ref.1

Sequence conflict

248

1

N → D in AAA88714. Ref.1

Sequence conflict

287

1

D → G in AAS56157. Ref.5

Sequence conflict

329

1

V → I in CAA24607. Ref.1

Sequence conflict

329

1

V → I in AAA88714. Ref.1

Secondary structure

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332

Helix Strand Turn

Details...

Beta strand

3 – 7

5

Helix

11 – 22

12

Beta strand

27 – 32

6

Helix

38 – 46

9

Turn

49 – 51

3

Beta strand

58 – 60

3

Beta strand

62 – 67

6

Beta strand

70 – 75

6

Helix

80 – 82

3

Turn

85 – 89

5

Beta strand

91 – 95

5

Beta strand

97 – 100

4

Helix

103 – 111

9

Beta strand

115 – 121

7

Beta strand

124 – 126

3

Turn

131 – 133

3

Helix

135 – 137

3

Beta strand

144 – 146

3

Helix

150 – 166

17

Beta strand

168 – 178

11

Beta strand

183 – 187

5

Helix

195 – 197

3

Helix

200 – 202

3

Beta strand

205 – 208

4

Helix

211 – 218

8

Helix

220 – 222

3

Beta strand

225 – 234

10

Beta strand

239 – 249

11

Helix

253 – 265

13

Turn

266 – 271

6

Beta strand

272 – 275

4

Helix

281 – 284

4

Beta strand

290 – 294

5

Helix

295 – 297

3

Beta strand

299 – 302

4

Beta strand

305 – 312

8

Helix

316 – 331

16

Sequences

	Sequence		Length	Mass (Da)
	P00359 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6CFFFEE7061BC36F	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

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] [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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 47-58. Strain: ATCC 204508 / S288c.
[7]	"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.
[8]	"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.
[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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"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-149; SER-178 AND SER-201, MASS SPECTROMETRY. Strain: YAL6B.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-175 AND SER-178, MASS SPECTROMETRY.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, MASS SPECTROMETRY.
[13]	"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-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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

DEBYG2. S55870.

RefSeq

NP_011708.3. NM_001181321.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3PYM	X-ray	2.00	A/B	1-332	[»]
4IQ8	X-ray	2.49	A	1-332	[»]

ProteinModelPortal

P00359.

SMR

P00359. Positions 1-332.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4309N.

IntAct

P00359. 94 interactions.

MINT

MINT-567189.

STRING

4932.YGR192C.

2D gel databases

COMPLUYEAST-2DPAGE

P00359.

SWISS-2DPAGE

P00359.

Proteomic databases

PaxDb

P00359.

PeptideAtlas

P00359.

PRIDE

P00359.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR192C; YGR192C; YGR192C.

GeneID

853106.

KEGG

sce:YGR192C.
sce:YGR198W.

Organism-specific databases

SGD

S000003424. TDH3.

Phylogenomic databases

eggNOG

COG0057.

GeneTree

ENSGT00690000101860.

HOGENOM

HOG000071678.

KO

K00134.

OMA

VSSDFCT.

OrthoDB

EOG4578GC.

Enzyme and pathway databases

SABIO-RK

P00359.

UniPathway

UPA00109; UER00184.

Gene expression databases

Genevestigator

P00359.

GermOnline

YGR192C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

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]

PANTHER

PTHR10836. PTHR10836. 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.

SMART

SM00846. Gp_dh_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01534. GAPDH-I. 1 hit.

PROSITE

PS00071. GAPDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

973112.

Entry information

Entry name

G3P3_YEAST

Accession

Primary (citable) accession number: P00359
Secondary accession number(s): D6VUX4, Q6Q5P9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 148 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program