G3PP1_ARATH
ID G3PP1_ARATH Reviewed; 422 AA.
AC Q9SAJ6;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase GAPCP1, chloroplastic;
DE EC=1.2.1.12;
DE AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase of plastid 1;
DE AltName: Full=NAD-dependent glyceraldehydephosphate dehydrogenase chloroplastic 1;
DE Flags: Precursor;
GN Name=GAPCP1; OrderedLocusNames=At1g79530; ORFNames=T8K14.5;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-236; HIS-263;
RP LYS-311 AND ARG-318.
RX PubMed=20107025; DOI=10.1104/pp.109.150458;
RA Munoz-Bertomeu J., Cascales-Minana B., Irles-Segura A., Mateu I.,
RA Nunes-Nesi A., Fernie A.R., Segura J., Ros R.;
RT "The plastidial glyceraldehyde-3-phosphate dehydrogenase is critical for
RT viable pollen development in Arabidopsis.";
RL Plant Physiol. 152:1830-1841(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-70, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-69, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in plastidial glycolytic pathway and plays a
CC specific role in glycolytic energy production in non-green plastids and
CC chloroplasts. Essential for breakdown of starch to form sucrose for
CC export to non-photosynthetic tissues, and to generate primary
CC metabolites for anabolic pathways such as fatty acid and amino acid
CC synthesis. Plays an important role in plant development by providing
CC substrates for the phosphorylated pathway of serine biosynthesis in
CC roots. Plays a crucial role in pollen development. Functionally
CC redundant with GAPCP2. {ECO:0000269|PubMed:19675149,
CC ECO:0000269|PubMed:20107025}.
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:19675149}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot and root vasculature, leaf veins
CC and vascular tissue of flowers and siliques.
CC {ECO:0000269|PubMed:15533878, ECO:0000269|PubMed:19675149}.
CC -!- INDUCTION: Repressed by darkness, but not by sucrose.
CC {ECO:0000269|PubMed:15533878}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. Gapcp1 and gapcp2 double mutants have severe dwarf
CC phenotypes with arrested root development and male sterility. Pollen
CC grains show shrunken and collapsed forms and cannot germinate.
CC {ECO:0000269|PubMed:19675149, ECO:0000269|PubMed:20107025}.
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; AC007202; AAD30223.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36260.1; -; Genomic_DNA.
DR EMBL; AK117920; BAC42558.1; -; mRNA.
DR EMBL; AF348583; AAK15554.1; -; mRNA.
DR PIR; F96826; F96826.
DR RefSeq; NP_178071.1; NM_106601.4.
DR AlphaFoldDB; Q9SAJ6; -.
DR SMR; Q9SAJ6; -.
DR BioGRID; 29510; 2.
DR IntAct; Q9SAJ6; 2.
DR STRING; 3702.AT1G79530.1; -.
DR iPTMnet; Q9SAJ6; -.
DR SwissPalm; Q9SAJ6; -.
DR PaxDb; Q9SAJ6; -.
DR PRIDE; Q9SAJ6; -.
DR ProMEX; Q9SAJ6; -.
DR ProteomicsDB; 230442; -.
DR EnsemblPlants; AT1G79530.1; AT1G79530.1; AT1G79530.
DR GeneID; 844291; -.
DR Gramene; AT1G79530.1; AT1G79530.1; AT1G79530.
DR KEGG; ath:AT1G79530; -.
DR Araport; AT1G79530; -.
DR TAIR; locus:2206435; AT1G79530.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; Q9SAJ6; -.
DR OMA; FMKFVSW; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; Q9SAJ6; -.
DR BRENDA; 1.2.1.12; 399.
DR PRO; PR:Q9SAJ6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAJ6; baseline and differential.
DR Genevisible; Q9SAJ6; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IMP:TAIR.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0080144; P:amino acid homeostasis; IMP:TAIR.
DR GO; GO:0048658; P:anther wall tapetum development; IMP:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:TAIR.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0080022; P:primary root 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 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 Acetylation; Chloroplast; Glycolysis; NAD; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 70..422
FT /note="Glyceraldehyde-3-phosphate dehydrogenase GAPCP1,
FT chloroplastic"
FT /id="PRO_0000422407"
FT REGION 50..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 236
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 96..97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 235..237
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 295..296
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 263
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 236
FT /note="C->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20107025"
FT MUTAGEN 263
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20107025"
FT MUTAGEN 311
FT /note="K->A: No effect on the activity."
FT /evidence="ECO:0000269|PubMed:20107025"
FT MUTAGEN 318
FT /note="R->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20107025"
SQ SEQUENCE 422 AA; 44831 MW; 3160AF8CDC2B30B2 CRC64;
MAFSSLLRSA ASYTVAAPRP DFFSSPASDH SKVLSSLGFS RNLKPSRFSS GISSSLQNGN
ARSVQPIKAT ATEVPSAVRR SSSSGKTKVG INGFGRIGRL VLRIATSRDD IEVVAVNDPF
IDAKYMAYML KYDSTHGNFK GSINVIDDST LEINGKKVNV VSKRDPSEIP WADLGADYVV
ESSGVFTTLS KAASHLKGGA KKVIISAPSA DAPMFVVGVN EHTYQPNMDI VSNASCTTNC
LAPLAKVVHE EFGILEGLMT TVHATTATQK TVDGPSMKDW RGGRGASQNI IPSSTGAAKA
VGKVLPELNG KLTGMAFRVP TSNVSVVDLT CRLEKGASYE DVKAAIKHAS EGPLKGILGY
TDEDVVSNDF VGDSRSSIFD ANAGIGLSKS FVKLVSWYDN EWGYSNRVLD LIEHMALVAA
SH
