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Protein

Glyceraldehyde-3-phosphate dehydrogenase 3

Gene

TDH3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase 1 (TDH1), Glyceraldehyde-3-phosphate dehydrogenase 2 (TDH2), Glyceraldehyde-3-phosphate dehydrogenase 3 (TDH3)
  2. Phosphoglycerate kinase (PGK1)
  3. Phosphoglycerate mutase 2 (GPM2), Phosphoglycerate mutase 3 (GPM3), Phosphoglycerate mutase 1 (GPM1)
  4. Enolase 2 (ENO2), Enolase-related protein 2 (ERR2), Enolase-related protein 3 (ERR3), Enolase-related protein 1 (ERR1), Enolase 1 (ENO1)
  5. Pyruvate kinase 2 (PYK2), Pyruvate kinase 1 (CDC19)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33NADBy similarity1
Binding sitei78NAD; via carbonyl oxygenBy similarity1
Active sitei150NucleophilePROSITE-ProRule annotation1
Sitei177Activates thiol group during catalysisBy similarity1
Binding sitei180Glyceraldehyde 3-phosphateBy similarity1
Binding sitei232Glyceraldehyde 3-phosphateBy similarity1
Binding sitei314NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 12NADBy similarity2

GO - Molecular functioni

  • glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: SGD
  • NAD binding Source: InterPro
  • NADP binding Source: InterPro
  • RNA binding Source: SGD

GO - Biological processi

  • apoptotic process Source: SGD
  • gluconeogenesis Source: SGD
  • glycolytic process Source: SGD
  • heme transport Source: SGD
  • 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.
ReactomeiR-SCE-70171. Glycolysis.
R-SCE-70263. Gluconeogenesis.
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
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR192C.
SGDiS000003424. TDH3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • fungal-type cell wall Source: SGD
  • lipid particle Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001455912 – 332Glyceraldehyde-3-phosphate dehydrogenase 3Add BLAST331

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei302PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP00359.
PRIDEiP00359.
TopDownProteomicsiP00359.

2D gel databases

COMPLUYEAST-2DPAGEP00359.
SWISS-2DPAGEP00359.

PTM databases

iPTMnetiP00359.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi33445. 158 interactors.
DIPiDIP-4309N.
IntActiP00359. 101 interactors.
MINTiMINT-8285236.

Structurei

Secondary structure

1332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Helixi11 – 22Combined sources12
Beta strandi27 – 32Combined sources6
Helixi38 – 46Combined sources9
Turni49 – 51Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi62 – 67Combined sources6
Beta strandi70 – 75Combined sources6
Helixi80 – 82Combined sources3
Turni85 – 89Combined sources5
Beta strandi91 – 95Combined sources5
Beta strandi97 – 100Combined sources4
Helixi103 – 111Combined sources9
Beta strandi115 – 121Combined sources7
Beta strandi124 – 126Combined sources3
Turni131 – 133Combined sources3
Helixi135 – 137Combined sources3
Beta strandi144 – 146Combined sources3
Helixi150 – 166Combined sources17
Beta strandi168 – 178Combined sources11
Beta strandi183 – 187Combined sources5
Helixi195 – 197Combined sources3
Helixi200 – 202Combined sources3
Beta strandi205 – 208Combined sources4
Helixi211 – 218Combined sources8
Helixi220 – 222Combined sources3
Beta strandi225 – 234Combined sources10
Beta strandi239 – 249Combined sources11
Helixi253 – 265Combined sources13
Turni266 – 271Combined sources6
Beta strandi272 – 275Combined sources4
Helixi281 – 284Combined sources4
Beta strandi290 – 294Combined sources5
Helixi295 – 297Combined sources3
Beta strandi299 – 302Combined sources4
Beta strandi305 – 312Combined sources8
Helixi316 – 331Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3PYMX-ray2.00A/B1-332[»]
4IQ8X-ray2.49A1-332[»]
ProteinModelPortaliP00359.
SMRiP00359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni149 – 151Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni209 – 210Glyceraldehyde 3-phosphate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
InParanoidiP00359.
KOiK00134.
OMAiTIFGHRN.
OrthoDBiEOG092C2MZH.

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]
SUPFAMiSSF51735. SSF51735. 1 hit.
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

        10         20         30         40         50
MVRVAINGFG RIGRLVMRIA LSRPNVEVVA LNDPFITNDY AAYMFKYDST
60 70 80 90 100
HGRYAGEVSH DDKHIIVDGK KIATYQERDP ANLPWGSSNV DIAIDSTGVF
110 120 130 140 150
KELDTAQKHI DAGAKKVVIT APSSTAPMFV MGVNEEKYTS DLKIVSNASC
160 170 180 190 200
TTNCLAPLAK VINDAFGIEE GLMTTVHSLT ATQKTVDGPS HKDWRGGRTA
210 220 230 240 250
SGNIIPSSTG AAKAVGKVLP ELQGKLTGMA FRVPTVDVSV VDLTVKLNKE
260 270 280 290 300
TTYDEIKKVV KAAAEGKLKG VLGYTEDAVV SSDFLGDSHS SIFDASAGIQ
310 320 330
LSPKFVKLVS WYDNEYGYST RVVDLVEHVA KA
Length:332
Mass (Da):35,747
Last modified:January 23, 2007 - v3
Checksum:i6CFFFEE7061BC36F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti136E → V in CAA24607 (PubMed:385592).Curated1
Sequence conflicti136E → V in AAA88714 (PubMed:385592).Curated1
Sequence conflicti248N → D in CAA24607 (PubMed:385592).Curated1
Sequence conflicti248N → D in AAA88714 (PubMed:385592).Curated1
Sequence conflicti287D → G in AAS56157 (PubMed:17322287).Curated1
Sequence conflicti329V → I in CAA24607 (PubMed:385592).Curated1
Sequence conflicti329V → I in AAA88714 (PubMed:385592).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3PYMX-ray2.00A/B1-332[»]
4IQ8X-ray2.49A1-332[»]
ProteinModelPortaliP00359.
SMRiP00359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33445. 158 interactors.
DIPiDIP-4309N.
IntActiP00359. 101 interactors.
MINTiMINT-8285236.

PTM databases

iPTMnetiP00359.

2D gel databases

COMPLUYEAST-2DPAGEP00359.
SWISS-2DPAGEP00359.

Proteomic databases

MaxQBiP00359.
PRIDEiP00359.
TopDownProteomicsiP00359.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YGR192C.
SGDiS000003424. TDH3.

Phylogenomic databases

GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
InParanoidiP00359.
KOiK00134.
OMAiTIFGHRN.
OrthoDBiEOG092C2MZH.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BioCyciYEAST:YGR192C-MONOMER.
ReactomeiR-SCE-70171. Glycolysis.
R-SCE-70263. Gluconeogenesis.
SABIO-RKP00359.

Miscellaneous databases

PROiP00359.

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]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 182 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.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.