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Protein

Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic

Gene

GAPC2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Binds DNA in vitro.By similarity1 Publication

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.PROSITE-ProRule annotation1 Publication

Enzyme regulationi

Inhibition by oxidized glutathione (GSSG), S-nitrosoglutathione (GSNO) and hydrogen peroxide.2 Publications

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 GAPC2, cytosolic (GAPC2), Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic (GAPC1)
  2. no protein annotated in this organism
  3. Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2 (At3g08590), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 (PGM1)
  4. Enolase 1, chloroplastic (ENO1), Cytosolic enolase 3 (ENO3), Bifunctional enolase 2/transcriptional activator (ENO2)
  5. Pyruvate kinase (At5g08570), Pyruvate kinase (At5g56350), Pyruvate kinase (At3g25960), Pyruvate kinase (At5g63680), Pyruvate kinase (F1I16_60), Plastidial pyruvate kinase 3, chloroplastic (PKP3), Pyruvate kinase (At3g52990), Pyruvate kinase (At2g36580), Pyruvate kinase, Probable pyruvate kinase, cytosolic isozyme (At4g26390), Pyruvate kinase (F8J2_160), Pyruvate kinase (At3g52990), Plastidial pyruvate kinase 2 (PKP2), Pyruvate kinase (T11I18.16), Pyruvate kinase (F1I16_220), Plastidial pyruvate kinase 1, chloroplastic (PKP1), Pyruvate kinase (At5g63680), Pyruvate kinase, Plastidial pyruvate kinase 4, chloroplastic (PKP4)
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 sitei37 – 371NADBy similarity
Binding sitei84 – 841NAD; via carbonyl oxygenBy similarity
Active sitei156 – 1561NucleophilePROSITE-ProRule annotation
Sitei183 – 1831Activates thiol group during catalysisBy similarity
Binding sitei186 – 1861Glyceraldehyde 3-phosphateBy similarity
Binding sitei238 – 2381Glyceraldehyde 3-phosphateBy similarity
Binding sitei320 – 3201NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 162NADBy similarity

GO - Molecular functioni

  • copper ion binding Source: TAIR
  • DNA binding Source: UniProtKB-KW
  • glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
  • NAD binding Source: InterPro
  • NADP binding Source: InterPro
  • zinc ion binding Source: TAIR

GO - Biological processi

  • defense response to bacterium Source: TAIR
  • gluconeogenesis Source: TAIR
  • glycolytic process Source: TAIR
  • response to cadmium ion Source: TAIR
  • response to oxidative stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

DNA-binding, NAD

Enzyme and pathway databases

ReactomeiR-ATH-70171. Glycolysis.
R-ATH-70263. Gluconeogenesis.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic (EC:1.2.1.12)
Alternative name(s):
NAD-dependent glyceraldehydephosphate dehydrogenase C subunit 2
Gene namesi
Name:GAPC2
Synonyms:GAPDH
Ordered Locus Names:At1g13440
ORF Names:T6J4.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G13440.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
  • chloroplast Source: TAIR
  • cytosol Source: TAIR
  • membrane Source: TAIR
  • mitochondrion Source: TAIR
  • nucleolus Source: TAIR
  • nucleus Source: TAIR
  • peroxisome Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolicPRO_0000420730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei156 – 1561S-glutathionyl cysteine; transient; alternate1 Publication
Modified residuei156 – 1561S-nitrosocysteine; transient; alternate1 Publication
Modified residuei160 – 1601S-nitrosocysteine; transient1 Publication

Post-translational modificationi

S-glutathionylation at Cys-156 in the presence of oxidized glutathione (GSSG). S-nitrosylation at Cys-156 and Cys-160 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.1 Publication

Keywords - PTMi

Glutathionylation, S-nitrosylation

Proteomic databases

PaxDbiQ9FX54.
PRIDEiQ9FX54.

2D gel databases

World-2DPAGE0003:Q9FX54.

PTM databases

iPTMnetiQ9FX54.

Expressioni

Gene expression databases

ExpressionAtlasiQ9FX54. baseline and differential.
GenevisibleiQ9FX54. AT.

Interactioni

Subunit structurei

Homotetramer (By similarity). Interacts with PLDDELTA.By similarity1 Publication

Protein-protein interaction databases

BioGridi23144. 15 interactions.
IntActiQ9FX54. 2 interactions.
STRINGi3702.AT1G13440.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FX54.
SMRiQ9FX54. Positions 5-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni155 – 1573Glyceraldehyde 3-phosphate bindingBy similarity
Regioni215 – 2162Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
InParanoidiQ9FX54.
KOiK00134.
OMAiWQHEASS.
PhylomeDBiQ9FX54.

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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FX54-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADKKIRIGI NGFGRIGRLV ARVVLQRDDV ELVAVNDPFI TTEYMTYMFK
60 70 80 90 100
YDSVHGQWKH HELKVKDDKT LLFGEKPVTV FGIRNPEDIP WGEAGADFVV
110 120 130 140 150
ESTGVFTDKD KAAAHLKGGA KKVVISAPSK DAPMFVVGVN EHEYKSDLDI
160 170 180 190 200
VSNASCTTNC LAPLAKVIND RFGIVEGLMT TVHSITATQK TVDGPSMKDW
210 220 230 240 250
RGGRAASFNI IPSSTGAAKA VGKVLPSLNG KLTGMSFRVP TVDVSVVDLT
260 270 280 290 300
VRLEKAATYD EIKKAIKEES EGKMKGILGY TEDDVVSTDF VGDNRSSIFD
310 320 330
AKAGIALSDK FVKLVSWYDN EWGYSSRVVD LIVHMSKA
Length:338
Mass (Da):36,913
Last modified:March 1, 2001 - v1
Checksum:i6EED7A21EBD51D64
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221R → K in BAH20011 (PubMed:19423640).Curated
Sequence conflicti262 – 2621I → V in BAH20011 (PubMed:19423640).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC011810 Genomic DNA. Translation: AAG09543.1.
CP002684 Genomic DNA. Translation: AEE29016.1.
AF410271 mRNA. Translation: AAK95257.1.
AY049259 mRNA. Translation: AAK83601.1.
AY090275 mRNA. Translation: AAL90936.1.
AK317337 mRNA. Translation: BAH20011.1.
RefSeqiNP_172801.1. NM_101214.3. [Q9FX54-1]
UniGeneiAt.23790.
At.24406.

Genome annotation databases

EnsemblPlantsiAT1G13440.1; AT1G13440.1; AT1G13440. [Q9FX54-1]
GeneIDi837904.
KEGGiath:AT1G13440.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC011810 Genomic DNA. Translation: AAG09543.1.
CP002684 Genomic DNA. Translation: AEE29016.1.
AF410271 mRNA. Translation: AAK95257.1.
AY049259 mRNA. Translation: AAK83601.1.
AY090275 mRNA. Translation: AAL90936.1.
AK317337 mRNA. Translation: BAH20011.1.
RefSeqiNP_172801.1. NM_101214.3. [Q9FX54-1]
UniGeneiAt.23790.
At.24406.

3D structure databases

ProteinModelPortaliQ9FX54.
SMRiQ9FX54. Positions 5-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23144. 15 interactions.
IntActiQ9FX54. 2 interactions.
STRINGi3702.AT1G13440.1.

PTM databases

iPTMnetiQ9FX54.

2D gel databases

World-2DPAGE0003:Q9FX54.

Proteomic databases

PaxDbiQ9FX54.
PRIDEiQ9FX54.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G13440.1; AT1G13440.1; AT1G13440. [Q9FX54-1]
GeneIDi837904.
KEGGiath:AT1G13440.

Organism-specific databases

TAIRiAT1G13440.

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
InParanoidiQ9FX54.
KOiK00134.
OMAiWQHEASS.
PhylomeDBiQ9FX54.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
ReactomeiR-ATH-70171. Glycolysis.
R-ATH-70263. Gluconeogenesis.

Miscellaneous databases

PROiQ9FX54.

Gene expression databases

ExpressionAtlasiQ9FX54. baseline and differential.
GenevisibleiQ9FX54. AT.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
    , 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.
  4. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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, GLUTATHIONYLATION AT CYS-156, S-NITROSYLATION AT CYS-156 AND CYS-160.
  6. "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.
  7. "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.

Entry informationi

Entry nameiG3PC2_ARATH
AccessioniPrimary (citable) accession number: Q9FX54
Secondary accession number(s): B9DGZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2013
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.