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Protein

Glyceraldehyde-3-phosphate dehydrogenase 1

Gene

TDH1

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

Pathway:iglycolysis

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 1 (ERR1), Enolase-related protein 3 (ERR3), 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331NADBy similarity
Binding sitei78 – 781NAD; via carbonyl oxygenBy similarity
Active sitei150 – 1501NucleophilePROSITE-ProRule annotation
Sitei177 – 1771Activates thiol group during catalysisBy similarity
Binding sitei180 – 1801Glyceraldehyde 3-phosphateBy similarity
Binding sitei232 – 2321Glyceraldehyde 3-phosphateBy similarity
Binding sitei314 – 3141NADBy similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

  • gluconeogenesis Source: SGD
  • glycolytic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciYEAST:YJL052W-MONOMER.
ReactomeiREACT_275254. Glycolysis.
REACT_286539. Gluconeogenesis.
SABIO-RKP00360.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase 1 (EC:1.2.1.12)
Short name:
GAPDH 1
Gene namesi
Name:TDH1
Synonyms:GPD1, SSS2
Ordered Locus Names:YJL052W
ORF Names:J1154
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL052W.
SGDiS000003588. TDH1.

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Glyceraldehyde-3-phosphate dehydrogenase 1PRO_0000145589Add
BLAST

Proteomic databases

MaxQBiP00360.
PaxDbiP00360.
PeptideAtlasiP00360.
PRIDEiP00360.

2D gel databases

SWISS-2DPAGEP00360.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi33703. 60 interactions.
DIPiDIP-4304N.
IntActiP00360. 23 interactions.
MINTiMINT-491516.

Structurei

3D structure databases

ProteinModelPortaliP00360.
SMRiP00360. Positions 1-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0057.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
InParanoidiP00360.
KOiK00134.
OMAiMIRIAIN.
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.

P00360-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRIAINGFG RIGRLVLRLA LQRKDIEVVA VNDPFISNDY AAYMVKYDST
60 70 80 90 100
HGRYKGTVSH DDKHIIIDGV KIATYQERDP ANLPWGSLKI DVAVDSTGVF
110 120 130 140 150
KELDTAQKHI DAGAKKVVIT APSSSAPMFV VGVNHTKYTP DKKIVSNASC
160 170 180 190 200
TTNCLAPLAK VINDAFGIEE GLMTTVHSMT ATQKTVDGPS HKDWRGGRTA
210 220 230 240 250
SGNIIPSSTG AAKAVGKVLP ELQGKLTGMA FRVPTVDVSV VDLTVKLEKE
260 270 280 290 300
ATYDQIKKAV KAAAEGPMKG VLGYTEDAVV SSDFLGDTHA SIFDASAGIQ
310 320 330
LSPKFVKLIS WYDNEYGYSA RVVDLIEYVA KA
Length:332
Mass (Da):35,750
Last modified:January 23, 2007 - v3
Checksum:i4C116C86EAF3DB70
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481E → A in CAA24609 (PubMed:6833300).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01302 Genomic DNA. Translation: CAA24609.1.
Z49327 Genomic DNA. Translation: CAA89343.1.
AY693001 Genomic DNA. Translation: AAT93020.1.
BK006943 Genomic DNA. Translation: DAA08747.1.
PIRiS56824. DEBYG3.
RefSeqiNP_012483.3. NM_001181485.3.

Genome annotation databases

EnsemblFungiiYJL052W; YJL052W; YJL052W.
GeneIDi853395.
KEGGisce:YJL052W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01302 Genomic DNA. Translation: CAA24609.1.
Z49327 Genomic DNA. Translation: CAA89343.1.
AY693001 Genomic DNA. Translation: AAT93020.1.
BK006943 Genomic DNA. Translation: DAA08747.1.
PIRiS56824. DEBYG3.
RefSeqiNP_012483.3. NM_001181485.3.

3D structure databases

ProteinModelPortaliP00360.
SMRiP00360. Positions 1-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33703. 60 interactions.
DIPiDIP-4304N.
IntActiP00360. 23 interactions.
MINTiMINT-491516.

2D gel databases

SWISS-2DPAGEP00360.

Proteomic databases

MaxQBiP00360.
PaxDbiP00360.
PeptideAtlasiP00360.
PRIDEiP00360.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL052W; YJL052W; YJL052W.
GeneIDi853395.
KEGGisce:YJL052W.

Organism-specific databases

EuPathDBiFungiDB:YJL052W.
SGDiS000003588. TDH1.

Phylogenomic databases

eggNOGiCOG0057.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
InParanoidiP00360.
KOiK00134.
OMAiMIRIAIN.
OrthoDBiEOG70W3Q6.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BioCyciYEAST:YJL052W-MONOMER.
ReactomeiREACT_275254. Glycolysis.
REACT_286539. Gluconeogenesis.
SABIO-RKP00360.

Miscellaneous databases

NextBioi973876.
PROiP00360.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 64-70 AND 218-225.
    Strain: ATCC 44827 / SKQ2N.
  6. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
  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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiG3P1_YEAST
AccessioniPrimary (citable) accession number: P00360
Secondary accession number(s): D6VWD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 165 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 120000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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 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.