G3PB_SPIOL
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 03-AUG-2022, entry version 135.
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; Chenopodiaceae; 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 + 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: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}.
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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 PDBsum; 2PKQ; -.
DR AlphaFoldDB; P12860; -.
DR SMR; P12860; -.
DR DIP; DIP-34904N; -.
DR IntAct; P12860; 2.
DR SABIO-RK; P12860; -.
DR UniPathway; UPA00116; -.
DR EvolutionaryTrace; P12860; -.
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 3D-structure; Calvin cycle; Chloroplast; Direct protein sequencing; NADP;
KW Oxidoreductase; Plastid; 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
