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P25858

- G3PC1_ARATH

UniProt

P25858 - G3PC1_ARATH

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Protein

Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic

Gene

GAPC1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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. 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.2 Publications

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.1 PublicationPROSITE-ProRule annotation

Enzyme regulationi

Inhibition by oxidized glutathione (GSSG), S-nitrosoglutathione (GSNO), hydrogen peroxide and sodium nitroprusside (SNP).4 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371NADBy similarity
Binding sitei84 – 841NAD; via carbonyl oxygenBy similarity
Active sitei156 – 1561Nucleophile
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

  1. copper ion binding Source: TAIR
  2. DNA binding Source: UniProtKB-KW
  3. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: TAIR
  4. glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity Source: TAIR
  5. NAD binding Source: InterPro
  6. NADP binding Source: InterPro

GO - Biological processi

  1. fruit development Source: TAIR
  2. gluconeogenesis Source: TAIR
  3. glycolytic process Source: TAIR
  4. response to cadmium ion Source: TAIR
  5. response to heat Source: TAIR
  6. response to hydrogen peroxide Source: TAIR
  7. response to oxidative stress Source: TAIR
  8. response to redox state Source: TAIR
  9. response to salt stress Source: TAIR
  10. response to sucrose Source: TAIR
  11. seed development Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis, Stress response

Keywords - Ligandi

DNA-binding, NAD

Enzyme and pathway databases

ReactomeiREACT_239253. Gluconeogenesis.
REACT_248260. Glycolysis.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic (EC:1.2.1.12)
Alternative name(s):
NAD-dependent glyceraldehydephosphate dehydrogenase C subunit 1
Gene namesi
Name:GAPC1
Synonyms:GAPC, GAPDH
Ordered Locus Names:At3g04120
ORF Names:T6K12.26
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G04120.

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. cytosol Source: TAIR
  4. membrane Source: TAIR
  5. mitochondrial envelope Source: TAIR
  6. mitochondrion Source: TAIR
  7. nucleus Source: TAIR
  8. plasma membrane Source: TAIR
  9. vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi156 – 1561C → S: Loss of activity. Loss of glutathionylation. 1 Publication
Mutagenesisi160 – 1601C → S: No effect on the activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolicPRO_0000145594Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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.1 Publication
Ubiquitinated.1 Publication

Keywords - PTMi

Glutathionylation, S-nitrosylation, Ubl conjugation

Proteomic databases

PaxDbiP25858.
PRIDEiP25858.

Expressioni

Tissue specificityi

Expressed in leaves, stems and siliques and at lower levels in roots and flowers.1 Publication

Inductioni

Not repressed by darkness or sucrose.1 Publication

Gene expression databases

ExpressionAtlasiP25858. baseline and differential.
GenevestigatoriP25858.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi4902. 9 interactions.
IntActiP25858. 2 interactions.
MINTiMINT-8060263.

Structurei

3D structure databases

ProteinModelPortaliP25858.
SMRiP25858. 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

eggNOGiCOG0057.
HOGENOMiHOG000071678.
InParanoidiP25858.
KOiK00134.
OMAiISNDKMK.
PhylomeDBiP25858.

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.

P25858-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADKKIRIGI NGFGRIGRLV ARVVLQRDDV ELVAVNDPFI TTEYMTYMFK
60 70 80 90 100
YDSVHGQWKH NELKIKDEKT LLFGEKPVTV FGIRNPEDIP WAEAGADYVV
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 VGKVLPALNG KLTGMSFRVP TVDVSVVDLT
260 270 280 290 300
VRLEKAATYD EIKKAIKEES EGKLKGILGY TEDDVVSTDF VGDNRSSIFD
310 320 330
AKAGIALSDK FVKLVSWYDN EWGYSSRVVD LIVHMSKA
Length:338
Mass (Da):36,914
Last modified:May 2, 2002 - v2
Checksum:i4186F65E1F1EE96F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271A → E in AAA32794. (PubMed:1916285)Curated
Sequence conflicti127 – 1271A → E in AAA32796. (PubMed:1916285)Curated
Sequence conflicti136 – 1361V → F in AAM65189. 1 PublicationCurated
Sequence conflicti260 – 2601D → E in AAA32794. (PubMed:1916285)Curated
Sequence conflicti260 – 2601D → E in AAA32796. (PubMed:1916285)Curated
Sequence conflicti325 – 3251S → N in AAM65189. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJQ1287.
RefSeqiNP_187062.1. NM_111283.3.
UniGeneiAt.22963.
At.24406.
At.71328.

Genome annotation databases

EnsemblPlantsiAT3G04120.1; AT3G04120.1; AT3G04120.
GeneIDi819567.
KEGGiath:AT3G04120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi JQ1287.
RefSeqi NP_187062.1. NM_111283.3.
UniGenei At.22963.
At.24406.
At.71328.

3D structure databases

ProteinModelPortali P25858.
SMRi P25858. Positions 5-337.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 4902. 9 interactions.
IntActi P25858. 2 interactions.
MINTi MINT-8060263.

Proteomic databases

PaxDbi P25858.
PRIDEi P25858.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G04120.1 ; AT3G04120.1 ; AT3G04120 .
GeneIDi 819567.
KEGGi ath:AT3G04120.

Organism-specific databases

TAIRi AT3G04120.

Phylogenomic databases

eggNOGi COG0057.
HOGENOMi HOG000071678.
InParanoidi P25858.
KOi K00134.
OMAi ISNDKMK.
PhylomeDBi P25858.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00184 .
Reactomei REACT_239253. Gluconeogenesis.
REACT_248260. Glycolysis.

Gene expression databases

ExpressionAtlasi P25858. baseline and differential.
Genevestigatori P25858.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR020831. 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 ]
PANTHERi PTHR10836. PTHR10836. 1 hit.
Pfami PF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000149. GAP_DH. 1 hit.
PRINTSi PR00078. G3PDHDRGNASE.
SMARTi SM00846. Gp_dh_N. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01534. GAPDH-I. 1 hit.
PROSITEi PS00071. GAPDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "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.
    , 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.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "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.
    , 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.
  6. "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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-321.
    Strain: cv. Columbia.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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].
  14. "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.
  15. "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.
  16. "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 nameiG3PC1_ARATH
AccessioniPrimary (citable) accession number: P25858
Secondary accession number(s): Q0WVE7
, Q42352, Q8LAS0, Q9M8W8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 2, 2002
Last modified: November 26, 2014
This is version 134 of the entry and version 2 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

External Data

Dasty 3