G3PA_PEA
ID G3PA_PEA Reviewed; 405 AA.
AC P12858;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic;
DE EC=1.2.1.13;
DE AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase subunit A;
DE Flags: Precursor;
GN Name=GAPA; Synonyms=GPA1;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Rosakrone; TISSUE=Seedling;
RX PubMed=2247465; DOI=10.1073/pnas.87.22.8918;
RA Liaud M.-F., Zhang D.-X., Cerff R.;
RT "Differential intron loss and endosymbiotic transfer of chloroplast
RT glyceraldehyde-3-phosphate dehydrogenase genes to the nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8918-8922(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Rosakrone; TISSUE=Seedling;
RX PubMed=2562762; DOI=10.1007/bf00027337;
RA Brinkmann H., Cerff R., Salomon M., Soll J.;
RT "Cloning and sequence analysis of cDNAs encoding the cytosolic precursors
RT of subunits GapA and GapB of chloroplast glyceraldehyde-3-phosphate
RT dehydrogenase from pea and spinach.";
RL Plant Mol. Biol. 13:81-94(1989).
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:0000250}.
CC -!- INTERACTION:
CC P12858; P12859: GAPB; NbExp=2; IntAct=EBI-15689968, EBI-15689988;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- MISCELLANEOUS: Plants contain two types of GAPDH: cytosolic forms which
CC participate in glycolysis and chloroplast forms which participate in
CC photosynthesis. All the 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; X52148; CAA36396.1; -; Genomic_DNA.
DR EMBL; X15190; CAA33264.1; -; mRNA.
DR PIR; S14243; DEPMNA.
DR AlphaFoldDB; P12858; -.
DR SMR; P12858; -.
DR DIP; DIP-29836N; -.
DR IntAct; P12858; 2.
DR PRIDE; P12858; -.
DR EnsemblPlants; Psat3g091720.1; Psat3g091720.1.cds; Psat3g091720.
DR Gramene; Psat3g091720.1; Psat3g091720.1.cds; Psat3g091720.
DR UniPathway; UPA00116; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
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 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 Calvin cycle; Chloroplast; NADP; Oxidoreductase; Plastid; Transit peptide.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT CHAIN 69..405
FT /note="Glyceraldehyde-3-phosphate dehydrogenase A,
FT chloroplastic"
FT /id="PRO_0000010423"
FT ACT_SITE 222
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 80..81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 221..223
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 280..281
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 249
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 194
FT /note="G -> R (in Ref. 2; CAA33264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 43338 MW; 667FD75FD3EA6430 CRC64;
MASATFSVAK PAIKANGKGF SEFSGLRNSS RHLPFSRKSS DDFHSLVTFQ TNAVGSSGGH
KKSLVVEAKQ LKVAINGFGR IGRNFLRCWH GRKDSPLDVI AINDTGGVKQ ASHLLKYDST
LGIFDADVKP VGTDGISVDG KVIKVVSDRN PANLPWKELG IDLVIEGTGV FVDREGAGRH
ITAGAKKVLI TAPGKGDIPT YVVGVNADAY THADDIISNA SCTTNCLAPF VKVLDQKFGI
IKGTMTTTHS YTGDQRLLDA SHRDLRRARA AALNIVPTST GAAKAVALVL PTLKGKLNGI
ALRVPTPNVS VVDLVVQVSK KTFAEEVNEA FRESAAKELT GILSVCDEPL VSVDFRCTDV
SSTVDSSLTM VMGDDLVKVI AWYDNEWGYS QRVVDLADIV ANNWK
