G3PB_PEA
ID G3PB_PEA Reviewed; 451 AA.
AC P12859;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 127.
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 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.
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] OF 5-451.
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 P12859; P12858: GAPA; NbExp=2; IntAct=EBI-15689988, EBI-15689968;
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; M55147; AAA84543.1; -; Genomic_DNA.
DR EMBL; X15188; CAA33262.1; -; mRNA.
DR PIR; S16507; DEPMNB.
DR AlphaFoldDB; P12859; -.
DR SMR; P12859; -.
DR DIP; DIP-29837N; -.
DR IntAct; P12859; 1.
DR PRIDE; P12859; -.
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..84
FT /note="Chloroplast"
FT CHAIN 85..451
FT /note="Glyceraldehyde-3-phosphate dehydrogenase B,
FT chloroplastic"
FT /id="PRO_0000010424"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 95..96
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 238..240
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 297..298
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 266
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 255
FT /note="F -> S (in Ref. 2; CAA33262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 48097 MW; C5D63CE37B19CE57 CRC64;
MATHAALAST RIPTNTRFPS KTSHSFPSQC ASKRLEVGEF SGLKSTSCIS YVHSARDSSF
YDVVAAQLTS KANGSTAVKG VTVAKLKVAI NGFGRIGRNF LRCWHGRKDS PLEVIVVNDS
GGVKNASHLL KYDSMLGTFK AEVKILNNET ITVDGKPIKV VSSRDPLKLP WAELGIDIVI
EGTGVFVDGP GAGKHIQAGA KKVIITAPAK GADIPTYVIG VNEQDYGHEV ADIISNASCT
TNCLAPFAKV LDEEFGIVKG TMTTTHSYTG DQRLLDASHR DLRRARAAAL NIVPTSTGAA
KAVSLVLPQL KGKLNGIALR VPTPNVSVVD LVVNVAKKGI SAEDVNAAFR KAAEGPLKGI
LDVCDVPLVS VDFRCSDVST TIDSSLTMVM GDDMVKVVAW YDNEWGYSQR VVDLAHLVAN
KWPGTPKVGS GDPLEDFCET NPADEECKVY E