ID G3PA_TOBAC Reviewed; 392 AA. AC P09043; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 02-SEP-2026, entry version 136. 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; Fragment; GN Name=GAPA; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3757034; DOI=10.1016/0092-8674(86)90367-3; RA Shih M.-C., Lazar G., Goodman H.M.; RT "Evidence in favor of the symbiotic origin of chloroplasts: primary RT structure and evolution of tobacco glyceraldehyde-3-phosphate RT dehydrogenases."; RL Cell 47:73-80(1986). CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + phosphate + NADP(+) = (2R)-3- CC phospho-glyceroyl phosphate + NADPH + H(+); 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M14417; AAA34075.1; -; mRNA. DR PIR; A24430; A24430. DR AlphaFoldDB; P09043; -. DR SMR; P09043; -. DR STRING; 4097.P09043; -. DR PaxDb; 4097-P09043; -. DR ProMEX; P09043; -. DR UniPathway; UPA00116; -. DR Proteomes; UP000790787; Unplaced. 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; IBA:GO_Central. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway. DR CDD; cd18126; GAPDH_I_C; 1. DR CDD; cd05214; GAPDH_I_N; 1. DR FunFam; 3.30.360.10:FF:000002; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000001; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 NCBIfam; TIGR01534; GAPDH-I; 1. DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00071; GAPDH; 1. PE 2: Evidence at transcript level; KW Calvin cycle; Chloroplast; NADP; Oxidoreductase; Plastid; KW Reference proteome; Transit peptide. FT TRANSIT <1..56 FT /note="Chloroplast" FT CHAIN 57..392 FT /note="Glyceraldehyde-3-phosphate dehydrogenase A, FT chloroplastic" FT /id="PRO_0000010427" FT ACT_SITE 209 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009" FT BINDING 67..68 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 136 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 208..210 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 239 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 254 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 267..268 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 290 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 372 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT SITE 236 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000250" FT NON_TER 1 SQ SEQUENCE 392 AA; 41863 MW; 35647D90B542D047 CRC64; NSSLQVSNKG FSEFSGLRTS SAIPFGRKTN DDLLSVVAFQ TSVIGGGNSK RGVVEAKLKV AINGFGRIGR NFLRCWHGRK DSPLDVIAIN DTGGVKQASH LLKYDSTLGI FDADVKPVGT DGISVDGKVI QVVSDRNPVN LPWGDLGIDL VIEGTGVFVD REGAGKHIQA GAKKVLITAP GKGDIPTYVV GVNADLYNPD EPIISNASCT TNCLAPFVKV LDQKFGIIKG TMTTTHSYTG DQRLLDASHR DLRRARAAAL NIVPTSTGAA KAVALSSQAL RGSSMALPLR VPTPNVSVVD LVVQVSKKTF AEEVNAAFRE AADKELKGIL DVCDEPLVSV DFRCSDVSST VDASLTMVMG DDMVKVIAWY DNEWGYSQRV VDLADIVANQ WK //