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P25858 (G3PC1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 GAPC1, cytosolic

EC=1.2.1.12
Alternative name(s):
NAD-dependent glyceraldehydephosphate dehydrogenase C subunit 1
Gene names
Name:GAPC1
Synonyms:GAPC, GAPDH
Ordered Locus Names:At3g04120
ORF Names:T6K12.26
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism. Involved in response to oxidative stress by mediating plant responses to abscisic acid (ABA) and water deficits through the activation of PLDDELTA and production of phosphatidic acid (PA), a multifunctional stress signaling lipid in plants. Required for full fertility. Binds DNA in vitro. Ref.12 Ref.17

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH. Ref.11

Enzyme regulation

Inhibition by oxidized glutathione (GSSG), S-nitrosoglutathione (GSNO), hydrogen peroxide and sodium nitroprusside (SNP). Ref.10 Ref.11 Ref.16 Ref.17

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

Subunit structure

Homotetramer By similarity. Interacts with PLDDELTA. Ref.17

Subcellular location

Cytoplasm. Nucleus Ref.11 Ref.15.

Tissue specificity

Expressed in leaves, stems and siliques and at lower levels in roots and flowers. Ref.9

Induction

Not repressed by darkness or sucrose. Ref.9 Ref.10 Ref.11 Ref.16 Ref.17

Post-translational modification

S-glutathionylation at Cys-156 in the presence of oxidized glutathione (GSSG). S-nitrosylation in the presence of S-nitrosoglutathione (GSNO) or sodium nitroprusside (SNP). These reactions may be both a protective mechanism against irreversible oxidation and a mean to store inhibited enzyme in a recoverable form. Glutathionylation is reversed by both glutaredoxins and thioredoxins in vitro.

Ubiquitinated.

Disruption phenotype

Delayed growth, small siliques with defects in fertility, and alterations of seed and fruit development. Reduced respiratory rates, pyruvate levels and Krebs cycle intermediates. Increased reactive oxygen species levels. Ref.12

Miscellaneous

Plants contain three types of GAPDH: NAD-dependent cytosolic forms which participate in glycolysis, NAD-dependent chloroplastic forms which participate in plastidic glycolysis and NADP-depedent chloroplastic forms which participate in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). All the forms are encoded by distinct genes.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
Stress response
   Cellular componentCytoplasm
Nucleus
   LigandDNA-binding
NAD
   Molecular functionOxidoreductase
   PTMGlutathionylation
S-nitrosylation
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfruit development

Inferred from mutant phenotype Ref.12. Source: TAIR

gluconeogenesis

Traceable author statement Ref.9. Source: TAIR

glycolysis

Inferred from direct assay Ref.12PubMed 23569110. Source: TAIR

response to cadmium ion

Inferred from expression pattern PubMed 16502469. Source: TAIR

response to heat

Inferred from expression pattern PubMed 8278495. Source: TAIR

response to hydrogen peroxide

Inferred from direct assay Ref.10. Source: TAIR

response to oxidative stress

Inferred from direct assay PubMed 12492832. Source: TAIR

response to redox state

Inferred from direct assay PubMed 23569110. Source: TAIR

response to salt stress

Inferred from expression pattern PubMed 17916636. Source: TAIR

response to sucrose

Inferred from expression pattern PubMed 8278495. Source: TAIR

seed development

Inferred from mutant phenotype Ref.12. Source: TAIR

   Cellular_componentapoplast

Inferred from direct assay PubMed 18538804. Source: TAIR

chloroplast

Inferred from direct assay PubMed 18431481. Source: TAIR

cytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

mitochondrial envelope

Inferred from direct assay PubMed 12953116. Source: TAIR

mitochondrion

Inferred from direct assay PubMed 12492832PubMed 14671022. Source: TAIR

nucleus

Inferred from direct assay PubMed 14617066. Source: TAIR

plasma membrane

Inferred from direct assay PubMed 17317660PubMed 17644812. Source: TAIR

vacuolar membrane

Inferred from direct assay PubMed 17151019. Source: TAIR

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from electronic annotation. Source: InterPro

copper ion binding

Inferred from direct assay PubMed 20018591. Source: TAIR

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

Traceable author statement PubMed 3055302. Source: TAIR

glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity

Inferred from direct assay Ref.12. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic
PRO_0000145594

Regions

Nucleotide binding15 – 162NAD By similarity
Region155 – 1573Glyceraldehyde 3-phosphate binding By similarity
Region215 – 2162Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1561Nucleophile
Binding site371NAD By similarity
Binding site841NAD; via carbonyl oxygen By similarity
Binding site1861Glyceraldehyde 3-phosphate By similarity
Binding site2381Glyceraldehyde 3-phosphate By similarity
Binding site3201NAD By similarity
Site1831Activates thiol group during catalysis By similarity

Amino acid modifications

Modified residue1561S-glutathionyl cysteine; transient; alternate
Modified residue1561S-nitrosocysteine; transient; alternate By similarity
Modified residue1601S-nitrosocysteine; transient By similarity

Experimental info

Mutagenesis1561C → S: Loss of activity. Loss of glutathionylation. Ref.16
Mutagenesis1601C → S: No effect on the activity. Ref.16
Sequence conflict1271A → E in AAA32794. Ref.1
Sequence conflict1271A → E in AAA32796. Ref.1
Sequence conflict1361V → F in AAM65189. Ref.7
Sequence conflict2601D → E in AAA32794. Ref.1
Sequence conflict2601D → E in AAA32796. Ref.1
Sequence conflict3251S → N in AAM65189. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P25858 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: 4186F65E1F1EE96F

FASTA33836,914
        10         20         30         40         50         60 
MADKKIRIGI NGFGRIGRLV ARVVLQRDDV ELVAVNDPFI TTEYMTYMFK YDSVHGQWKH 

        70         80         90        100        110        120 
NELKIKDEKT LLFGEKPVTV FGIRNPEDIP WAEAGADYVV ESTGVFTDKD KAAAHLKGGA 

       130        140        150        160        170        180 
KKVVISAPSK DAPMFVVGVN EHEYKSDLDI VSNASCTTNC LAPLAKVIND RFGIVEGLMT 

       190        200        210        220        230        240 
TVHSITATQK TVDGPSMKDW RGGRAASFNI IPSSTGAAKA VGKVLPALNG KLTGMSFRVP 

       250        260        270        280        290        300 
TVDVSVVDLT VRLEKAATYD EIKKAIKEES EGKLKGILGY TEDDVVSTDF VGDNRSSIFD 

       310        320        330 
AKAGIALSDK FVKLVSWYDN EWGYSSRVVD LIVHMSKA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and chromosomal mapping of nuclear genes encoding chloroplast and cytosolic glyceraldehyde-3-phosphate-dehydrogenase from Arabidopsis thaliana."
Shih M.-C., Heinrich P., Goodman H.M.
Gene 104:133-138(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]Erratum
Shih M.-C., Heinrich P., Goodman H.M.
Gene 119:317-319(1992) [PubMed] [Europe PMC] [Abstract]
[3]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[7]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs."
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C., Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R., Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J. expand/collapse author list , Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.
Plant J. 9:101-124(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-321.
Strain: cv. Columbia.
[9]"Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana."
Marri L., Sparla F., Pupillo P., Trost P.
J. Exp. Bot. 56:73-80(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[10]"Proteomic identification of glyceraldehyde 3-phosphate dehydrogenase as an inhibitory target of hydrogen peroxide in Arabidopsis."
Hancock J.T., Henson D., Nyirenda M., Desikan R., Harrison J., Lewis M., Hughes J., Neill S.J.
Plant Physiol. Biochem. 43:828-835(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Regulation of plant cytosolic glyceraldehyde 3-phosphate dehydrogenase isoforms by thiol modifications."
Holtgrefe S., Gohlke J., Starmann J., Druce S., Klocke S., Altmann B., Wojtera J., Lindermayr C., Scheibe R.
Physiol. Plantarum 133:211-228(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION.
[12]"Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase."
Rius S.P., Casati P., Iglesias A.A., Gomez-Casati D.F.
Plant Physiol. 148:1655-1667(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[13]"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.
[14]"Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS].
[15]"Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to altered root development and affects the sugar and amino acid balance in Arabidopsis."
Munoz-Bertomeu J., Cascales-Minana B., Mulet J.M., Baroja-Fernandez E., Pozueta-Romero J., Kuhn J.M., Segura J., Ros R.
Plant Physiol. 151:541-558(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro."
Bedhomme M., Adamo M., Marchand C.H., Couturier J., Rouhier N., Lemaire S.D., Zaffagnini M., Trost P.
Biochem. J. 445:337-347(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, GLUTATHIONYLATION AT CYS-156, MUTAGENESIS OF CYS-156 AND CYS-160.
[17]"Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with phospholipase Ddelta to transduce hydrogen peroxide signals in the Arabidopsis response to stress."
Guo L., Devaiah S.P., Narasimhan R., Pan X., Zhang Y., Zhang W., Wang X.
Plant Cell 24:2200-2212(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH PLDDELTA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64116 mRNA. Translation: AAA32794.1.
M64119 Genomic DNA. Translation: AAA32796.1.
AC016829 Genomic DNA. Translation: AAF26801.1.
CP002686 Genomic DNA. Translation: AEE74039.1.
AY052267 mRNA. Translation: AAK97737.1.
AY060521 mRNA. Translation: AAL31134.1.
AY140084 mRNA. Translation: AAM98225.1.
AK226804 mRNA. Translation: BAE98901.1.
AY087651 mRNA. Translation: AAM65189.1.
F20074 mRNA. Translation: CAA23391.1.
PIRJQ1287.
RefSeqNP_187062.1. NM_111283.3.
UniGeneAt.22963.
At.24406.
At.71328.

3D structure databases

ProteinModelPortalP25858.
SMRP25858. Positions 5-337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid4902. 9 interactions.
IntActP25858. 1 interaction.
MINTMINT-8060263.

Proteomic databases

PaxDbP25858.
PRIDEP25858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G04120.1; AT3G04120.1; AT3G04120.
GeneID819567.
KEGGath:AT3G04120.

Organism-specific databases

TAIRAT3G04120.

Phylogenomic databases

eggNOGCOG0057.
HOGENOMHOG000071678.
InParanoidP25858.
KOK00134.
OMAINEPFMD.
PhylomeDBP25858.
ProtClustDBPLN02358.

Enzyme and pathway databases

UniPathwayUPA00109; UER00184.

Gene expression databases

ArrayExpressP25858.
GenevestigatorP25858.

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...

Entry information

Entry nameG3PC1_ARATH
AccessionPrimary (citable) accession number: P25858
Secondary accession number(s): Q0WVE7 expand/collapse secondary AC list , Q42352, Q8LAS0, Q9M8W8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 2, 2002
Last modified: April 16, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names