G3PA1_ARATH
ID G3PA1_ARATH Reviewed; 396 AA.
AC P25856; Q41184; Q9LSE6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic;
DE EC=1.2.1.13;
DE AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase A subunit 1;
DE Flags: Precursor;
GN Name=GAPA1; Synonyms=GAPA; OrderedLocusNames=At3g26650;
GN ORFNames=MLJ15.4, MLJ15_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 [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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia; TISSUE=Shoot;
RX PubMed=8932388; DOI=10.1093/nar/24.21.4313;
RA Quigley F., Dao P., Cottet A., Mache R.;
RT "Sequence analysis of an 81 kb contig from Arabidopsis thaliana chromosome
RT III.";
RL Nucleic Acids Res. 24:4313-4318(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [8]
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 [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 60-396 IN COMPLEX WITH NAD, AND
RP SUBUNIT.
RX PubMed=20516587; DOI=10.1107/s1744309110013527;
RA Fermani S., Sparla F., Marri L., Thumiger A., Pupillo P., Falini G.,
RA Trost P.;
RT "Structure of photosynthetic glyceraldehyde-3-phosphate dehydrogenase
RT (isoform A4) from Arabidopsis thaliana in complex with NAD.";
RL Acta Crystallogr. F 66:621-626(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 60-396 IN COMPLEX WITH NAD, AND
RP SUBUNIT.
RX PubMed=22514274; DOI=10.1074/jbc.m112.350355;
RA Fermani S., Trivelli X., Sparla F., Thumiger A., Calvaresi M., Marri L.,
RA Falini G., Zerbetto F., Trost P.;
RT "Conformational selection and folding-upon-binding of intrinsically
RT disordered protein CP12 regulate photosynthetic enzymes assembly.";
RL J. Biol. Chem. 287:21372-21383(2012).
CC -!- FUNCTION: Involved in the photosynthetic reductive pentose phosphate
CC pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-
CC diphosphoglycerate by NADPH (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.13;
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Tetramer of either four A chains (GAPDH 2) or two A and two B
CC chains (GAPDH 1). {ECO:0000269|PubMed:20516587,
CC ECO:0000269|PubMed:22514274}.
CC -!- INTERACTION:
CC P25856; Q9LZP9: CP12-2; NbExp=4; IntAct=EBI-1554434, EBI-449218;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral
CC membrane protein. Plastid, chloroplast stroma.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and stems.
CC {ECO:0000269|PubMed:15533878}.
CC -!- INDUCTION: Repressed by darkness and sucrose.
CC {ECO:0000269|PubMed:15533878}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10209.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M64114; AAD10209.1; ALT_INIT; mRNA.
DR EMBL; M64117; AAA32793.1; -; Genomic_DNA.
DR EMBL; S45910; AAB23532.1; -; Genomic_DNA.
DR EMBL; X98130; CAA66816.1; -; Genomic_DNA.
DR EMBL; AB026648; BAB01730.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77191.1; -; Genomic_DNA.
DR EMBL; AY058140; AAL25556.1; -; mRNA.
DR EMBL; AY058107; AAL24215.1; -; mRNA.
DR EMBL; AF428431; AAL16200.1; -; mRNA.
DR EMBL; AY075637; AAL91645.1; -; mRNA.
DR EMBL; AY142053; AAM98317.1; -; mRNA.
DR PIR; JQ1285; JQ1285.
DR RefSeq; NP_566796.2; NM_113576.4.
DR PDB; 3K2B; X-ray; 2.60 A; A/B/C/D/E/F/G/H/O/Q=60-396.
DR PDB; 3QV1; X-ray; 2.00 A; A/B/C/D/E/F=60-396.
DR PDB; 3RVD; X-ray; 2.70 A; A/B/C/D/E/F/G/H/O/Q=61-396.
DR PDB; 6KEZ; X-ray; 3.50 A; A/B/C/D/E/F/G/H=61-396.
DR PDBsum; 3K2B; -.
DR PDBsum; 3QV1; -.
DR PDBsum; 3RVD; -.
DR PDBsum; 6KEZ; -.
DR AlphaFoldDB; P25856; -.
DR SMR; P25856; -.
DR BioGRID; 7607; 9.
DR IntAct; P25856; 2.
DR MINT; P25856; -.
DR STRING; 3702.AT3G26650.1; -.
DR iPTMnet; P25856; -.
DR SWISS-2DPAGE; P25856; -.
DR World-2DPAGE; 0003:P25856; -.
DR PaxDb; P25856; -.
DR PRIDE; P25856; -.
DR ProteomicsDB; 228893; -.
DR EnsemblPlants; AT3G26650.1; AT3G26650.1; AT3G26650.
DR GeneID; 822277; -.
DR Gramene; AT3G26650.1; AT3G26650.1; AT3G26650.
DR KEGG; ath:AT3G26650; -.
DR Araport; AT3G26650; -.
DR TAIR; locus:2090802; AT3G26650.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_2_1; -.
DR InParanoid; P25856; -.
DR OMA; SMLTPTN; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; P25856; -.
DR BioCyc; ARA:AT3G26650-MON; -.
DR BioCyc; MetaCyc:AT3G26650-MON; -.
DR BRENDA; 1.2.1.13; 399.
DR UniPathway; UPA00116; -.
DR EvolutionaryTrace; P25856; -.
DR PRO; PR:P25856; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P25856; baseline and differential.
DR Genevisible; P25856; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0099080; C:supramolecular complex; IDA:CAFA.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:CAFA.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0051287; F:NAD binding; IDA:CAFA.
DR GO; GO:0050661; F:NADP binding; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0051289; P:protein homotetramerization; IDA:CAFA.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; NAS:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP: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; PTHR43148; PTHR43148; 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; Calvin cycle; Chloroplast; Membrane; NADP; Oxidoreductase;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 61..396
FT /note="Glyceraldehyde-3-phosphate dehydrogenase GAPA1,
FT chloroplastic"
FT /id="PRO_0000010416"
FT ACT_SITE 213
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 71..72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:20516587,
FT ECO:0000269|PubMed:22514274"
FT BINDING 95
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:20516587,
FT ECO:0000269|PubMed:22514274"
FT BINDING 140
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:20516587,
FT ECO:0000269|PubMed:22514274"
FT BINDING 212..214
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 271..272
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:20516587,
FT ECO:0000269|PubMed:22514274"
FT SITE 240
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 172
FT /note="I -> M (in Ref. 1; AAA32793/AAD10209 and 3;
FT CAA66816)"
FT /evidence="ECO:0000305"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:3QV1"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 119..129
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3QV1"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 213..229
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 231..241
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3QV1"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 273..280
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3QV1"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 301..311
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:3QV1"
FT TURN 328..333
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:3QV1"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:3QV1"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:3QV1"
FT HELIX 378..393
FT /evidence="ECO:0007829|PDB:3QV1"
SQ SEQUENCE 396 AA; 42490 MW; FFD7FD662FB222FC CRC64;
MASVTFSVPK GFTEFSGLRS SSASLPFGKK LSSDEFVSIV SFQTSAMGSS GGYRKGVTEA
KLKVAINGFG RIGRNFLRCW HGRKDSPLDI IAINDTGGVK QASHLLKYDS TLGIFDADVK
PSGETAISVD GKIIQVVSNR NPSLLPWKEL GIDIVIEGTG VFVDREGAGK HIEAGAKKVI
ITAPGKGDIP TYVVGVNADA YSHDEPIISN ASCTTNCLAP FVKVLDQKFG IIKGTMTTTH
SYTGDQRLLD ASHRDLRRAR AAALNIVPTS TGAAKAVALV LPNLKGKLNG IALRVPTPNV
SVVDLVVQVS KKTFAEEVNA AFRDSAEKEL KGILDVCDEP LVSVDFRCSD FSTTIDSSLT
MVMGDDMVKV IAWYDNEWGY SQRVVDLADI VANNWK
