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P25858

- G3PC1_ARATH

UniProt

P25858 - G3PC1_ARATH

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
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis, Stress response

    Keywords - Ligandi

    DNA-binding, NAD

    Enzyme and pathway databases

    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

    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

    ArrayExpressiP25858.
    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

    MADKKIRIGI NGFGRIGRLV ARVVLQRDDV ELVAVNDPFI TTEYMTYMFK    50
    YDSVHGQWKH NELKIKDEKT LLFGEKPVTV FGIRNPEDIP WAEAGADYVV 100
    ESTGVFTDKD KAAAHLKGGA KKVVISAPSK DAPMFVVGVN EHEYKSDLDI 150
    VSNASCTTNC LAPLAKVIND RFGIVEGLMT TVHSITATQK TVDGPSMKDW 200
    RGGRAASFNI IPSSTGAAKA VGKVLPALNG KLTGMSFRVP TVDVSVVDLT 250
    VRLEKAATYD EIKKAIKEES EGKLKGILGY TEDDVVSTDF VGDNRSSIFD 300
    AKAGIALSDK FVKLVSWYDN EWGYSSRVVD LIVHMSKA 338
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .

    Gene expression databases

    ArrayExpressi P25858.
    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

    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: October 1, 2014
    This is version 132 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