ID G3PB_SPIOL Reviewed; 451 AA. AC P12860; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 02-SEP-2026, entry version 147. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase B, chloroplastic; DE EC=1.2.1.13; DE AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase subunit B; DE Flags: Precursor; GN Name=GAPB; Synonyms=GPB1; OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Amaranthaceae; Chenopodioideae; Anserineae; Spinacia. OX NCBI_TaxID=3562; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC 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). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8980499; DOI=10.1007/bf00019102; RA Baalmann E., Scheibe R., Cerff R., Martin W.; RT "Functional studies of chloroplast glyceraldehyde-3-phosphate dehydrogenase RT subunits A and B expressed in Escherichia coli: formation of highly active RT A4 and B4 homotetramers and evidence that aggregation of the B4 complex is RT mediated by the B subunit carboxy terminus."; RL Plant Mol. Biol. 32:505-513(1996). RN [3] RP PROTEIN SEQUENCE OF 83-451. RX PubMed=2223845; DOI=10.1016/0167-4838(90)90119-z; RA Ferri G., Stoppini M., Meloni M.L., Zapponi M.C., Iadarola P.; RT "Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid RT sequence of the subunits from isoenzyme I and structural relationship with RT isoenzyme II."; RL Biochim. Biophys. Acta 1041:36-42(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 84-451 IN COMPLEX WITH NADP, AND RP SUBUNIT. RX PubMed=17573533; DOI=10.1073/pnas.0611636104; RA Fermani S., Sparla F., Falini G., Martelli P.L., Casadio R., Pupillo P., RA Ripamonti A., Trost P.; RT "Molecular mechanism of thioredoxin regulation in photosynthetic A2B2- RT glyceraldehyde-3-phosphate dehydrogenase."; RL Proc. Natl. Acad. Sci. U.S.A. 104:11109-11114(2007). 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:0000269|PubMed:17573533}. 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; X15189; CAA33263.1; -; mRNA. DR EMBL; L76553; AAD10218.1; -; mRNA. DR PIR; S05553; DESPGB. DR PDB; 2PKQ; X-ray; 3.60 A; O/Q/T=84-451. DR PDB; 7Q53; EM; 6.30 A; O/Q=84-422. DR PDB; 7Q54; EM; 8.90 A; A/C/O/Q=1-451. DR PDB; 7Q55; EM; 5.70 A; A/C/E/G/I/K/O/Q=1-451. DR PDB; 7Q56; EM; 7.10 A; A/C/E/G/I/K/O/Q=84-451. DR PDB; 7Q57; EM; 13.00 A; A/C/E/G/I/K/M/O/Q/S=1-451. DR PDB; 9I06; EM; 3.20 A; A/C/E/G/I/K/O/Q=84-451. DR PDB; 9I07; EM; 3.10 A; A/C/E/G/I/K/O/Q=84-451. DR PDB; 9I3S; EM; 7.20 A; A/C/E/G/I/K/M/O/Q/S=84-451. DR AlphaFoldDB; P12860; -. DR EMDB; EMD-13824; -. DR EMDB; EMD-13825; -. DR EMDB; EMD-13826; -. DR EMDB; EMD-13827; -. DR EMDB; EMD-13828; -. DR EMDB; EMD-52552; -. DR EMDB; EMD-52553; -. DR EMDB; EMD-52614; -. DR SMR; P12860; -. DR DIP; DIP-34904N; -. DR IntAct; P12860; 2. DR SABIO-RK; P12860; -. DR UniPathway; UPA00116; -. DR EvolutionaryTrace; P12860; -. DR Proteomes; UP000813463; 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 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. DR PDBsum; 2PKQ; -. DR PDBsum; 7Q53; -. DR PDBsum; 7Q54; -. DR PDBsum; 7Q55; -. DR PDBsum; 7Q56; -. DR PDBsum; 7Q57; -. DR PDBsum; 9I06; -. DR PDBsum; 9I07; -. DR PDBsum; 9I3S; -. PE 1: Evidence at protein level; KW 3D-structure; Calvin cycle; Chloroplast; Direct protein sequencing; NADP; KW Oxidoreductase; Plastid; Reference proteome; Transit peptide. FT TRANSIT 1..83 FT /note="Chloroplast" FT CHAIN 84..451 FT /note="Glyceraldehyde-3-phosphate dehydrogenase B, FT chloroplastic" FT /id="PRO_0000010426" FT ACT_SITE 238 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009" FT BINDING 94..95 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17573533" FT BINDING 118 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17573533" FT BINDING 163 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17573533" FT BINDING 237..239 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 268 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 283 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 296..297 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 319 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 402 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17573533" FT SITE 265 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000250" SQ SEQUENCE 451 AA; 48126 MW; 45D826A6DA5B4837 CRC64; MASHAALAPS RIPASTRLAS KASQQYSFLT QCSFKRLDVA DFSGLRSSNS VTFTREASFH DVIAAQLTTK PTGAAPVRGE TVAKLKVAIN GFGRIGRNFL RCWHGRKDSP LDVVVVNDSG GVKSATHLLK YDSILGTFKA DVKIIDNETF SIDGKPIKVV SNRDPLKLPW AELGIDIVIE GTGVFVDGPG AGKHIQAGAK KVIITAPAKG SDIPTYVVGV NEKDYGHDVA NIISNASCTT NCLAPFVKVL DEELGIVKGT MTTTHSYTGD QRLLDASHRD LRRARAAALN IVPTSTGAAK AVSLVLPQLK GKLNGIALRV PTPNVSVVDL VVNIEKVGVT AEDVNNAFRK AAAGPLKGVL DVCDIPLVSV DFRCSDFSST IDSSLTMVMG GDMVKVVAWY DNEWGYSQRV VDLADLVANK WPGLEGSVAS GDPLEDFCKD NPADEECKLY E //