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P00360 (G3P1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceEvidence 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.7.

Miscellaneous

There are three genes for G3PDH in yeast.

Present with 120000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Glyceraldehyde-3-phosphate dehydrogenase 1
PRO_0000145589

Regions

Nucleotide binding11 – 122NAD By similarity
Region149 – 1513Glyceraldehyde 3-phosphate binding By similarity
Region209 – 2102Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1501Nucleophile By similarity
Binding site331NAD By similarity
Binding site781NAD; via carbonyl oxygen By similarity
Binding site1801Glyceraldehyde 3-phosphate By similarity
Binding site2321Glyceraldehyde 3-phosphate By similarity
Binding site3141NAD By similarity
Site1771Activates thiol group during catalysis By similarity

Experimental info

Sequence conflict2481E → A in CAA24609. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00360 [UniParc].

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

FASTA33235,750
        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 

« Hide

References

« Hide '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] [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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
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. expand/collapse author list , 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.
[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]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01302 Genomic DNA. Translation: CAA24609.1.
Z49327 Genomic DNA. Translation: CAA89343.1.
AY693001 Genomic DNA. Translation: AAT93020.1.
BK006943 Genomic DNA. Translation: DAA08747.1.
PIRDEBYG3. S56824.
RefSeqNP_012483.3. NM_001181485.3.

3D structure databases

ProteinModelPortalP00360.
SMRP00360. Positions 1-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33703. 59 interactions.
DIPDIP-4304N.
IntActP00360. 23 interactions.
MINTMINT-491516.
STRING4932.YJL052W.

2D gel databases

SWISS-2DPAGEP00360.

Proteomic databases

MaxQBP00360.
PaxDbP00360.
PeptideAtlasP00360.
PRIDEP00360.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL052W; YJL052W; YJL052W.
GeneID853395.
KEGGsce:YJL052W.

Organism-specific databases

SGDS000003588. TDH1.

Phylogenomic databases

eggNOGCOG0057.
GeneTreeENSGT00720000108591.
HOGENOMHOG000071678.
KOK00134.
OMAALRVVIC.
OrthoDBEOG70W3Q6.

Enzyme and pathway databases

BioCycYEAST:YJL052W-MONOMER.
SABIO-RKP00360.
UniPathwayUPA00109; UER00184.

Gene expression databases

GenevestigatorP00360.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR020831. 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]
PANTHERPTHR10836. PTHR10836. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio973876.
PROP00360.

Entry information

Entry nameG3P1_YEAST
AccessionPrimary (citable) accession number: P00360
Secondary accession number(s): D6VWD1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways