G3PC1_ARATH
ID G3PC1_ARATH Reviewed; 338 AA.
AC P25858; Q0WVE7; Q42352; Q8LAS0; Q9M8W8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic {ECO:0000303|PubMed:1916285};
DE EC=1.2.1.12 {ECO:0000255|PROSITE-ProRule:PRU10009, ECO:0000269|PubMed:18298409};
DE AltName: Full=NAD-dependent glyceraldehydephosphate dehydrogenase C subunit 1 {ECO:0000303|PubMed:15533878};
GN Name=GAPC1 {ECO:0000303|PubMed:15533878};
GN Synonyms=GAPC {ECO:0000303|PubMed:15533878},
GN GAPDH {ECO:0000303|PubMed:1916285};
GN OrderedLocusNames=At3g04120 {ECO:0000312|Araport:AT3G04120};
GN ORFNames=T6K12.26 {ECO:0000312|EMBL:AAF26801.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1916285; DOI=10.1016/0378-1119(91)90242-4;
RA Shih M.-C., Heinrich P., Goodman H.M.;
RT "Cloning and chromosomal mapping of nuclear genes encoding chloroplast and
RT cytosolic glyceraldehyde-3-phosphate-dehydrogenase from Arabidopsis
RT thaliana.";
RL Gene 104:133-138(1991).
RN [2]
RP ERRATUM OF PUBMED:1916285.
RX PubMed=1398114; DOI=10.1016/0378-1119(92)90290-6;
RA Shih M.-C., Heinrich P., Goodman H.M.;
RL Gene 119:317-319(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-321.
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15533878; DOI=10.1093/jxb/eri020;
RA Marri L., Sparla F., Pupillo P., Trost P.;
RT "Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate
RT dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana.";
RL J. Exp. Bot. 56:73-80(2005).
RN [10]
RP ACTIVITY REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16289945; DOI=10.1016/j.plaphy.2005.07.012;
RA Hancock J.T., Henson D., Nyirenda M., Desikan R., Harrison J., Lewis M.,
RA Hughes J., Neill S.J.;
RT "Proteomic identification of glyceraldehyde 3-phosphate dehydrogenase as an
RT inhibitory target of hydrogen peroxide in Arabidopsis.";
RL Plant Physiol. Biochem. 43:828-835(2005).
RN [11]
RP CATALYTIC ACTIVITY, PATHWAY, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=18298409; DOI=10.1111/j.1399-3054.2008.01066.x;
RA Holtgrefe S., Gohlke J., Starmann J., Druce S., Klocke S., Altmann B.,
RA Wojtera J., Lindermayr C., Scheibe R.;
RT "Regulation of plant cytosolic glyceraldehyde 3-phosphate dehydrogenase
RT isoforms by thiol modifications.";
RL Physiol. Plantarum 133:211-228(2008).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18820081; DOI=10.1104/pp.108.128769;
RA Rius S.P., Casati P., Iglesias A.A., Gomez-Casati D.F.;
RT "Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic
RT NAD-dependent glyceraldehyde-3-phosphate dehydrogenase.";
RL Plant Physiol. 148:1655-1667(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=19675149; DOI=10.1104/pp.109.143701;
RA Munoz-Bertomeu J., Cascales-Minana B., Mulet J.M., Baroja-Fernandez E.,
RA Pozueta-Romero J., Kuhn J.M., Segura J., Ros R.;
RT "Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to
RT altered root development and affects the sugar and amino acid balance in
RT Arabidopsis.";
RL Plant Physiol. 151:541-558(2009).
RN [15]
RP ACTIVITY REGULATION, GLUTATHIONYLATION AT CYS-156, AND MUTAGENESIS OF
RP CYS-156 AND CYS-160.
RX PubMed=22607208; DOI=10.1042/bj20120505;
RA Bedhomme M., Adamo M., Marchand C.H., Couturier J., Rouhier N.,
RA Lemaire S.D., Zaffagnini M., Trost P.;
RT "Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase
RT from the model plant Arabidopsis thaliana is reversed by both glutaredoxins
RT and thioredoxins in vitro.";
RL Biochem. J. 445:337-347(2012).
RN [16]
RP FUNCTION, AND INTERACTION WITH FBA6 AND VDAC3.
RX PubMed=23316205; DOI=10.3389/fpls.2012.00284;
RA Wojtera-Kwiczor J., Gross F., Leffers H.M., Kang M., Schneider M.,
RA Scheibe R.;
RT "Transfer of a redox-signal through the cytosol by redox-dependent
RT microcompartmentation of glycolytic enzymes at mitochondria and actin
RT cytoskeleton.";
RL Front. Plant Sci. 3:284-284(2012).
RN [17]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH PLDDELTA.
RX PubMed=22589465; DOI=10.1105/tpc.111.094946;
RA Guo L., Devaiah S.P., Narasimhan R., Pan X., Zhang Y., Zhang W., Wang X.;
RT "Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with
RT phospholipase Ddelta to transduce hydrogen peroxide signals in the
RT Arabidopsis response to stress.";
RL Plant Cell 24:2200-2212(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 5-338, AND ACTIVE SITE.
RA Zaffagnini M., Fermani S., Calvaresi M., Marchand C., Orru R.,
RA Iommarini L., Sparla F., Bottoni F., Falini G., Lemaire S.D., Trost P.;
RT "Structural determinants of sulfenic acid reactivity in the active site of
RT cytoplasmic and photosynthetic Arabidopsis GAPDHs from Arabidopsis
RT thaliana.";
RL Submitted (MAR-2015) to the PDB data bank.
RN [19]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-121 AND LYS-231,
RP INTERACTION WITH DPB3-1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=32651385; DOI=10.1038/s41467-020-17311-4;
RA Kim S.-C., Guo L., Wang X.;
RT "Nuclear moonlighting of cytosolic glyceraldehyde-3-phosphate dehydrogenase
RT regulates Arabidopsis response to heat stress.";
RL Nat. Commun. 11:3439-3439(2020).
CC -!- FUNCTION: Key enzyme in glycolysis that catalyzes the first step of the
CC pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-
CC phospho-D-glyceroyl phosphate. Essential for the maintenance of
CC cellular ATP levels and carbohydrate metabolism. Required for full
CC fertility (PubMed:18820081). Involved in response to oxidative stress
CC by mediating plant responses to abscisic acid (ABA) and water deficits
CC through the activation of PLDDELTA and production of phosphatidic acid
CC (PA), a multifunctional stress signaling lipid in plants
CC (PubMed:22589465). Associates with FBA6 to the outer mitochondrial
CC membrane, in a redox-dependent manner, leading to binding and bundling
CC of actin. Actin binding and bundling occurs under oxidizing conditions
CC and is reversible under reducing conditions. May be part of a redox-
CC dependent retrograde signal transduction network for adaptation upon
CC oxidative stress (PubMed:23316205). Binds DNA in vitro. Together with
CC DNA polymerase II subunit B3-1 (DPB3-1) and GAPC2, enhances heat
CC tolerance and promotes the expression of heat-inducible genes
CC (PubMed:32651385). {ECO:0000269|PubMed:18820081,
CC ECO:0000269|PubMed:22589465, ECO:0000269|PubMed:23316205,
CC ECO:0000269|PubMed:32651385}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009,
CC ECO:0000269|PubMed:18298409};
CC -!- ACTIVITY REGULATION: Inhibition by oxidized glutathione (GSSG), S-
CC nitrosoglutathione (GSNO), hydrogen peroxide and sodium nitroprusside
CC (SNP). {ECO:0000269|PubMed:16289945, ECO:0000269|PubMed:18298409,
CC ECO:0000269|PubMed:22589465, ECO:0000269|PubMed:22607208}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000269|PubMed:18298409}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with PLDDELTA
CC (PubMed:22589465). Interacts with FBA6 and VDAC3 (PubMed:23316205).
CC Binds to DPB3-1/NF-YC10 in response to heat-stress; this interaction
CC promotes DPB3-1/NF-YC10 DNA-binding ability to its target promoter
CC (PubMed:32651385). {ECO:0000250|UniProtKB:P54226,
CC ECO:0000269|PubMed:22589465, ECO:0000269|PubMed:23316205,
CC ECO:0000269|PubMed:32651385}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32651385}. Nucleus
CC {ECO:0000269|PubMed:32651385}. Note=Accumulates in the nucleus under
CC heat stress. {ECO:0000269|PubMed:32651385}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and siliques and at
CC lower levels in roots and flowers. {ECO:0000269|PubMed:15533878}.
CC -!- INDUCTION: Not repressed by darkness or sucrose.
CC {ECO:0000269|PubMed:15533878}.
CC -!- PTM: S-glutathionylation at Cys-156 in the presence of oxidized
CC glutathione (GSSG). S-nitrosylation in the presence of S-
CC nitrosoglutathione (GSNO) or sodium nitroprusside (SNP). These
CC reactions may be both a protective mechanism against irreversible
CC oxidation and a mean to store inhibited enzyme in a recoverable form.
CC Glutathionylation is reversed by both glutaredoxins and thioredoxins in
CC vitro. {ECO:0000269|PubMed:22607208}.
CC -!- DISRUPTION PHENOTYPE: Delayed growth, small siliques with defects in
CC fertility, and alterations of seed and fruit development
CC (PubMed:18820081). Reduced respiratory rates, pyruvate levels and Krebs
CC cycle intermediates (PubMed:18820081). Increased reactive oxygen
CC species levels (PubMed:18820081). The double mutant gapc1 gapc2 has an
CC impaired ability to enhance heat tolerance of seedlings and to promote
CC the expression of heat-inducible genes (PubMed:32651385).
CC {ECO:0000269|PubMed:18820081, ECO:0000269|PubMed:32651385}.
CC -!- MISCELLANEOUS: Plants contain three types of GAPDH: NAD-dependent
CC cytosolic forms which participate in glycolysis, NAD-dependent
CC chloroplastic forms which participate in plastidic glycolysis and NADP-
CC dependent chloroplastic forms which participate in the photosynthetic
CC reductive pentose phosphate pathway (Calvin-Benson cycle). All the
CC forms are encoded by distinct genes.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M64116; AAA32794.1; -; mRNA.
DR EMBL; M64119; AAA32796.1; -; Genomic_DNA.
DR EMBL; AC016829; AAF26801.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74039.1; -; Genomic_DNA.
DR EMBL; AY052267; AAK97737.1; -; mRNA.
DR EMBL; AY060521; AAL31134.1; -; mRNA.
DR EMBL; AY140084; AAM98225.1; -; mRNA.
DR EMBL; AK226804; BAE98901.1; -; mRNA.
DR EMBL; AY087651; AAM65189.1; -; mRNA.
DR EMBL; F20074; CAA23391.1; -; mRNA.
DR PIR; JQ1287; JQ1287.
DR RefSeq; NP_187062.1; NM_111283.4.
DR PDB; 4Z0H; X-ray; 2.30 A; O/R=5-338.
DR PDB; 6QUN; X-ray; 3.00 A; O/R=5-338.
DR PDB; 6QUQ; X-ray; 2.99 A; O/R=5-338.
DR PDBsum; 4Z0H; -.
DR PDBsum; 6QUN; -.
DR PDBsum; 6QUQ; -.
DR AlphaFoldDB; P25858; -.
DR SMR; P25858; -.
DR BioGRID; 4902; 11.
DR IntAct; P25858; 2.
DR MINT; P25858; -.
DR STRING; 3702.AT3G04120.1; -.
DR iPTMnet; P25858; -.
DR MetOSite; P25858; -.
DR PaxDb; P25858; -.
DR PRIDE; P25858; -.
DR ProteomicsDB; 228892; -.
DR EnsemblPlants; AT3G04120.1; AT3G04120.1; AT3G04120.
DR GeneID; 819567; -.
DR Gramene; AT3G04120.1; AT3G04120.1; AT3G04120.
DR KEGG; ath:AT3G04120; -.
DR Araport; AT3G04120; -.
DR TAIR; locus:2103085; AT3G04120.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; P25858; -.
DR OMA; HETYKGE; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; P25858; -.
DR BRENDA; 1.2.1.12; 399.
DR UniPathway; UPA00109; UER00184.
DR PRO; PR:P25858; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P25858; baseline and differential.
DR Genevisible; P25858; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity; IDA:TAIR.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0006094; P:gluconeogenesis; TAS:TAIR.
DR GO; GO:0006096; P:glycolytic process; IDA:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0051775; P:response to redox state; IDA:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Glutathionylation; Glycolysis; NAD;
KW Nucleus; Oxidoreductase; Reference proteome; S-nitrosylation;
KW Stress response.
FT CHAIN 1..338
FT /note="Glyceraldehyde-3-phosphate dehydrogenase GAPC1,
FT cytosolic"
FT /id="PRO_0000145594"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000269|Ref.18"
FT BINDING 15..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 155..157
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 186
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 215..216
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 238
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 183
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT MOD_RES 156
FT /note="S-glutathionyl cysteine; transient; alternate"
FT /evidence="ECO:0000269|PubMed:22607208"
FT MOD_RES 156
FT /note="S-nitrosocysteine; transient; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9FX54"
FT MOD_RES 160
FT /note="S-nitrosocysteine; transient"
FT /evidence="ECO:0000250|UniProtKB:Q9FX54"
FT MUTAGEN 121
FT /note="K->A: In GAPCmut; compromised heat-induced nuclear
FT accumulation leading to impaired ability to enhance heat
FT tolerance; when associated with A-231."
FT /evidence="ECO:0000269|PubMed:32651385"
FT MUTAGEN 156
FT /note="C->S: Loss of activity. Loss of glutathionylation."
FT /evidence="ECO:0000269|PubMed:22607208"
FT MUTAGEN 160
FT /note="C->S: No effect on the activity."
FT /evidence="ECO:0000269|PubMed:22607208"
FT MUTAGEN 231
FT /note="K->A: In GAPCmut; compromised heat-induced nuclear
FT accumulation leading to impaired ability to enhance heat
FT tolerance; when associated with A-121."
FT /evidence="ECO:0000269|PubMed:32651385"
FT CONFLICT 127
FT /note="A -> E (in Ref. 1; AAA32794/AAA32796)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="V -> F (in Ref. 7; AAM65189)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="D -> E (in Ref. 1; AAA32794/AAA32796)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="S -> N (in Ref. 7; AAM65189)"
FT /evidence="ECO:0000305"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:4Z0H"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:4Z0H"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4Z0H"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:4Z0H"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:4Z0H"
FT TURN 272..277
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:4Z0H"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:4Z0H"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:4Z0H"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:4Z0H"
SQ SEQUENCE 338 AA; 36914 MW; 4186F65E1F1EE96F CRC64;
MADKKIRIGI NGFGRIGRLV ARVVLQRDDV ELVAVNDPFI TTEYMTYMFK YDSVHGQWKH
NELKIKDEKT LLFGEKPVTV FGIRNPEDIP WAEAGADYVV ESTGVFTDKD KAAAHLKGGA
KKVVISAPSK DAPMFVVGVN EHEYKSDLDI VSNASCTTNC LAPLAKVIND RFGIVEGLMT
TVHSITATQK TVDGPSMKDW RGGRAASFNI IPSSTGAAKA VGKVLPALNG KLTGMSFRVP
TVDVSVVDLT VRLEKAATYD EIKKAIKEES EGKLKGILGY TEDDVVSTDF VGDNRSSIFD
AKAGIALSDK FVKLVSWYDN EWGYSSRVVD LIVHMSKA
