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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
 
 
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